RESEARCH GROUPS
PAGES
GENERAL PAGES
Groupleader: Irmgard Sinning
Irmgard Sinning
Structural Biology
select submenu:
Research
Prestigious medal from the State of Bavaria for Irmi Sinning
Leibniz-Prize 2014 awarded to Irmgard Sinning
Featured in nature Crystallography at 100 issue
Our mission
Our research aims at the understanding of fundamental cellular processes at atomic detail. Our key interests are the molecular mechanisms of protein homeostasis with focus on cotranslational protein folding, maturation and targeting. Defects in these processes can lead to numerous diseases including neurodegenerative disorders and cancer, which are a threat to our aging society. RNA-protein complexes here include ribosomes and the SRP system. Intrigued by RNA turnover and the importance of non-coding RNAs, we recently embarked on the analysis of a novel exosome adaptor complex. Membrane protein biogenesis extends our long-standing interest in protein targeting. All these processes depend on precisely orchestrated interactions of the proteins and macromolecular assemblies involved with nucleic acids, proteins, membrane lipids and other ligands. We address these topics by a broad methodological spectrum firmly routed by our expertise in macromolecular structure determination.
Our approach
Structural information is the basis to understand the function of macromolecular complexes and their dynamic interplay. We employ integrated structural biology with high-resolution structure determination by cryo-EM and X-ray crystallography in combination with biochemical and biophysical tools (e.g. BLI, MST, ITC, DSF, MALS, HDX-MS, XL-MS, SAXS). State of the art expression and purification strategies are the basis for our studies. Our model systems range from bacteria to eukaryotes and include our pet-eukaryote, the thermophilic fungus Chaetomium thermophilum. With HDcryoNET and the crystallization platform we established a powerful scientific infrastructure.
Cotranslational processes
Ribosomes are among the largest cellular machines and translate the information embedded in the mRNA into polypeptide sequences. However, the activity of ribosomes is not merely restricted to protein synthesis and to ensuring a high fidelity of translation. They are also crucial players in the modification, folding, assembly and membrane-insertion of newly-synthesized polypeptides. Ribosomes provide a binding platform for a whole network of machineries and thereby determine also the fate of nascent polypeptides. The interaction of these factors with the nascent chain requires precise spatio-temporal coordination as many of them interact already with short nascent chains and use overlapping sites nearby the ribosomal tunnel exit. They can be divided into three main classes: transport factors that assist in ER membrane targeting and insertion of membrane proteins (the SRP/SR/Sec61 pathway), chaperones that assist in correct protein folding (NAC, RAC/Ssb), and enzymes involved in nascent chain modification (MetAPs, NATs).
Protein targeting: SRP pathway:
Membrane proteins comprise more than 25% of the cellular proteome and their function depends on insertion into the correct target membrane. Cotranslational targeting by the signal recognition particle (SRP) pathway elegantly couples membrane protein synthesis with membrane insertion by the Sec translocon, and avoids exposure of hydrophobic transmembrane segments prone to aggregation. SRP is a universally conserved protein/RNA complex and the SRP pathway is controlled by a unique set of GTP binding proteins (Kempf et al. 2018; Wild et al. 2016; Montoya et al. 1997), which are regulated by the SRP RNA (reviewed in: Wild et al. 2019; Bange & Sinning 2013). Our goal is to deduce the molecular and structural framework of this multistep regulatory pathway that ensures the fidelity of protein transport. Analysing the first mutations in human SRP54 that cause severe congenital neutropenia as well as Shwachman-Diamond-like disease syndrome is a beautiful example of a detailed QSAR-type study. We showed a critical destabilization of the GTPase that eliminates targeting complex formation with the SRP receptor (Juaire et al. 2021). After showing how SRP RNA remodeling by SRP68/72 supports SRP function in elongation arrest and protein translocation (Grotwinkel et al. 2014; Becker et al, 2017), we recently succeeded in the large scale reconstitution of the complete human SRP system (Wild et al. 2019) opening new avenues for detailed studies.
Protein folding: RAC/Ssb:
Chaperones are essential in promoting correct protein folding in all domains of life. In yeast, the ribosome-associated complex (RAC) consists of the Hsp70 member Ssz1 and its Hsp40 partner Zuo1, which together with Ssb form a functional chaperone triad promoting co-translational folding of nascent chains (reviewed in: Zhang et al. 2017). For a long time, understanding RAC/Ssb function was impeded by the lack of structural information. A previous cryo-EM structure showed the position of yeast RAC at the ribosome, however the limited resolution did not allow to position individual protein domains (Zhang et al. 2014). While it was previously shown that the Ssb ATPase is activated only by the J-domain present in Zuo1, mechanistic details remained unresolved. Using proteins from our thermophilic model organism Chaetomium thermophilum, we obtained first insights into Ssb and RAC (Gumiero et al. 2016; Leidig et al 2013) and showed that Ssb interacts with ribosomal RNA and proteins at the tunnel exit by a conserved cluster of positively charged residues at its C-terminus (Gumiero et al. 2016). By structure determination of the RAC core we could show that the non-canonical Hsp70 protein Ssz1 does contain a substrate-binding domain (SBD). However, it lacks the helical lid domain, and the b-sandwich domain (SBDb) is complemented by the Zuo1 N-terminus (Zhang et al. 2020; Weyer et al. 2017). RAC and Ssb cooperate in a relay system at the ribosome to ensure productive nascent chain handover to Ssb (Zhang et al. 2020). One of the current goals is therefore to resolve mechanistic details of nascent chain recognition and handover in the RAC/Ssb relay.
Protein modification: MAPs and NATs:
A vast majority of nascent polypeptides in eukaryotes experience removal of the N-terminal methionine by ribosome-associated methionine-aminopeptidases (MAPs). Several protein factors that share the MAP-fold, but have no enzymatic activity occupy the putative MAP binding site. These include the ribosome-biogenesis factor Arx1 (Kater et al. 2017; Bradatsch et al. 2007) and Ebp1, which plays an important role in cancer regulation (Wild et al. 2020; Kowalinski et al. 2007). While structural information on 80S/MAP interaction is still missing, the eukaryote specific expansion segment 27 (ES27) seems to play an important role in orchestrating these proteins. Current studies using single-particle cryo-EM address this point.
N-terminal acetylation of nascent protein chains is one of the most common co-translational modifications in eukaryotes. Over 80% of all cytosolic proteins in mammals and more than 40% of all proteins in the yeast Saccharomyces cerevisiae are acetylated by Nα-terminal acetyltransferase complexes (NATs). The precise physiological role of this modification is still not established. However, it has been implicated in protein complex assembly, protein targeting, turnover and quality control. Five different NATs (NatA to NatE) modify each a distinct selection of cellular proteins due to different substrate specificities. NATs consist of at least two subunits, i.e. a ribosomal adapter (auxiliary subunit) and the catalytic subunit, which bind close to the ribosomal tunnel exit. However, the activity of NatA, which has the largest set of substrates, is regulated by additional factors: Naa50 and HypK. We showed that HypK in vitro serves by inhibiting NatA activity (Weyer et al. 2017) and that Naa50 has different, organism-specific roles in NatA regulation (Weidenhausen et a. 2021). NatB differs in substrate specificity and in catalytic activity of Naa20 alone (without its ribosome adaptor) (Layer et al. 2021; Huber et al. 2020). A long-term goal is to dissect the interplay between these enzymes and chaperones on nascent chains emerging from a translating ribosome.
Membrane protein insertion: the GET pathway
Targeting and insertion of membrane proteins into the correct membrane presents a challenge for the chaperones and machinery involved. The SRP system relies on the presence of an N-terminal signal sequence that is recognized in context of a translating ribosome. However, a subset of membrane proteins involved in important physiological processes ranging from intracellular trafficking to protein degradation and programmed cell death lack such a signal sequence. Instead they carry their targeting signal at the C-terminus and are therefore termed tail-anchored (TA) proteins. These proteins are targeted to the ER post-translationally by the GET pathway (guided entry of tail-anchored proteins). Such post-translational system requires a whole chaperone cascade to direct the TA proteins safely to the ER membrane for insertion. While the components of the GET pathway have been identified in the last decade, the molecular and structural framework especially of the ER insertion steps was lagging far behind our understanding e.g. of the SRP/Sec system. We set out to fill this gap by determining key structures on the involved machinery starting with the Get3 chaperone (Bozkurt et al. 2009) and its interaction with the Get1/Get2 insertase (Denic et al 2013; Stefer et al. 2011). Our recent cryo-EM structure of the human GET insertase (McDowell et al. 2020) shows a lipid-stabilized heterotetramer with a membrane-embedded hydrophilic groove and an unanticipated, conserved cytoplasmic helix, and reveals a striking structural homology between Get1 homologs and their bacterial counterpart YidC (McDowell et al. 2021). These structural details are the basis for further studies to understand the mechanisms of TA protein insertion and the role of dynamic membrane remodeling by insertase/lipid interactions.
Download BZH Report Sinning 2014-2016
CV
| 1989 | PhD (Biochemistry), University of Munich, with H. Michel (MPI Martinsried) |
| 1989-1991 | Postdoc with H. Michel (Biochemistry/Structural Biology), MPI-Biophysics Frankfurt |
| 1991-1993 | Postdoc with T.A. Jones (Structural Biology), BMC University of Uppsala, Sweden |
| 1994-1999 | Group Leader (Structural Biology Programme), EMBL Heidelberg |
| 2000- | C4/W3 Professor for Biochemistry/Structural Biology at the Heidelberg University Biochemistry Center (BZH) |
| 2006-2009 | Director of the Heidelberg University Biochemistry Center (BZH) |
| 2010- | Board of Directors of the Heidelberg University Biochemistry Center (BZH) |
| 2010 | Elected EMBO Member |
| 2010 | Elected Member of Leopoldina |
| 2016 | Elected member of Heidelberg Academy of Sciences and Humanities |
| 2019 | Elected member of Berlin-Brandenburgische Akademie der Wissenschaften (BBAW) |
Lab Members
Silke Adrian
TA
TA
Lab:Room 526
/ Phone: +49 6221 54-4787
Office:Room 526 a
/ Phone: +49 6221 54-4787
Mail:silke.adrian@bzh.uni-heidelberg.de
Gaetano D’Urso
postdoc
postdoc
Lab:Room 524
/ Phone: +49 6221 54-4784
Mail:gaetano.durso@bzh.uni-heidelberg.de
Eddye Javier Figueroa Márquez
PhD student
PhD student
Lab:Room 526
/ Phone: +49 6221 54-4787
Office:Room 526
/ Phone: +49 6221 54-4787
Mail:eddye.marquez@bzh.uni-heidelberg.de
Pietro Ivan Giammarinaro
postdoc
postdoc
Lab:Room 524
/ Phone: +49 6221 54-4784
Office:Room 506
/ Phone: +49 6221 54-4788
Mail:pietro.giammarinaro@bzh.uni-heidelberg.de
.jpg)
Astrid Hendricks
TA
TA
Lab:Room 524 a
/ Phone: +49 6221 54-4784
Office:Room 524 a
/ Phone: +49 6221 54-4784
Mail:astrid.hendricks@bzh.uni-heidelberg.de
Elke Herwig
TA
TA
Lab:Room 526
/ Phone: +49 6221 54-4789
Office:Room 526 b
/ Phone: +49 6221 54-4789
Mail:elke.herwig@bzh.uni-heidelberg.de
Matteo Hofmann
PhD student
PhD student
Lab:Room 524
/ Phone: +49 6221 54-4786
Office:Room 524
/ Phone: +49 6221 54-4786
Mail:matteo.hofmann@bzh.uni-heidelberg.de
Marius Klein
PhD student
PhD student
Lab:Room 524
/ Phone: +49 6221 54-4782
Office:Room 524
/ Phone: +49 6221 54-4782
Mail:marius.klein@bzh.uni-heidelberg.de
Britta Klem
TA
TA
Lab:Room 524c
/ Phone: +49 6221 54-4789
/ Phone: +49 6221 54-4786
Mail:britta.klem@bzh.uni-heidelberg.de
Jürgen Kopp
scientific staff
scientific staff
Lab:Room 265
/ Phone: +49 6221 54-4112
Office:Room 267
/ Phone: +49 6221 54-4481
Mail:juergen.kopp@bzh.uni-heidelberg.de
Leiter Kristallisationsplattform Cell Networks
Romina Ines Minen
postdoc
postdoc
Lab:Room 526
/ Phone: +49 6221 54-4796
Mail:romina.minen@bzh.uni-heidelberg.de
Ludwig Nücker
scientific staff
scientific staff
Office:Room 108
/ Phone: +49 6221 54-4783
Mail:lutz.nuecker@bzh.uni-heidelberg.de
Marina Pelzl
TA
TA
Lab:Room 524
/ Phone: +49 6221 54-4786
/ Phone: +49 6221 54-4786
Mail:marina.pelzl@bzh.uni-heidelberg.de
Auch im Raum 521 unter -4342 erreichbar!
Merlin Schwan
PhD student
PhD student
Lab:Room 526
/ Phone: +49 6221 54-4796
Office:Room 526
/ Phone: +49 6221 54-4796
Mail:merlin.schwan@bzh.uni-heidelberg.de
Claudia Siegmann
TA
TA
Lab:Room 266
Office:Room 265
/ Phone: +49 6221 54-4112
Mail:claudia.siegmann@bzh.uni-heidelberg.de
Mitarbeiterin Kristallisationsplattform Cell Networks
Gunter Stier
others
others
Lab:Room 526
/ Phone: +49 6221 54-4789
Office:Room 526 b
/ Phone: +49 6221 54-4789
Mail:gunter.stier@bzh.uni-heidelberg.de
Can Wang
postdoc
postdoc
Lab:Room 524
/ Phone: +49 6221 54-4782
Office:Room 506
/ Phone: +49 6221 54-4788
Mail:can.wang@bzh.uni-heidelberg.de
Anja Weber
secretary
secretary
Office:Room 507
/ Phone: +49 6221 54-4780
Mail:anja.weber@bzh.uni-heidelberg.de
.jpg)
Klemens Wild
staff scientist
staff scientist
Office:Room 509
/ Phone: +49 6221 54-4785
Mail:klemens.wild@bzh.uni-heidelberg.de
Publications
DEAD-box RNA helicases act as nucleotide exchange factors for casein kinase 2, Sci Signal 16: eabp8923. doi: doi.org/10.1126/scisignal.abp8923.
Fatti, E., Hirth, A., Švorinić, A., Günther, M., Cruciat, C.M., Stier, G., Acebron, S.P., Papageorgiou, D., Sinning, I., Krijgsveld, J., Höfer , T. & Niehrs, C. (2023)
Mechanistic insights into RNA surveillance by the canonical poly(A) polymerase Pla1 of the MTREC complex, Nat Commun. 14: 772. doi: doi.org/10.1038/s41467-023-36402-6. Soni, K., Sivadas, A., Horváth, A., Dobrev, N., Hayashi, R., Kiss, L., Simon, B., Wild, K. & Sinning*, I, Fischer*, T. (2023)
Methionine aminopeptidase 2 and its autoproteolysis product have different binding sites on the ribosome, bioRxiv doi:https://doi.org/10.1101/2023.04.06. 535065. Klein, M.A., Wild, K., Kisonaite, M. & Sinning, I. (2023)
Structural inventory of cotranslational protein folding by the eukaryotic RAC complex, Structural inventory of cotranslational protein folding by the eukaryotic RAC complex, Nat. Struct. Mol. Biol. Apr 20. doi: doi.org/10.1038/s41594-023-00973-1 (online ahead of print). Kišonaitė, M., Wild, K., Lapouge, K., Valentín Gesé, G., Kellner, N., Hurt, E. & Sinning, I. (2023)
Trim-Away degrades lysine-less substrates without requiring ligase autoubiquitination, Nat. Commun. 14: 2160. doi: doi.org/10.1038/s41467-023-37504-x. Kiss, L., Rhinesmith, T., Dickson, C.F., Weidenhausen, J., Smyly, S., Luptak, J., Yang, J.C., Maslen, S.L., Sinning, I., Neuhaus, D., Clift, D. & James, L.C. (2023)
Antibacterial peptide CyclomarinA creates toxicity by deregulating the Mycobacterium tuberculosis ClpC1-ClpP1P2 protease. J. Biol. Chem. 298:102202. doi: https://doi.org/10.1016/j.jbc.2022.102202. Taylor, G., Frommherz, Y., Katikaridis, P., Layer, D., Sinning, I., Carroni, M., Weber-Ban, E. & Mogk, A. (2022)
Cryo-EM insights into tail-anchored membrane protein biogenesis in eukaryotes, Curr. Opin. Struct. Biol. 75: 102428. doi: https://doi.org/10.1016/j.sbi.2022.102428. Sinning, I. and McDowell, M.A. (2022)
Extended N-Terminal Acetyltransferase Naa50 in Filamentous Fungi Adds to Naa50 Diversity. Int J Mol Sci. 2022 Sep 16;23(18):10805. doi: doi.org/10.3390/ijms231810805. PMID: 36142717; PMCID: PMC9500918. Weidenhausen J, Kopp J, Ruger-Herreros C, Stein F, Haberkant P, Lapouge K, Sinning I (2022)
High-resolution structures of a thermophilic eukaryotic 80S ribosome reveal atomistic details of translocation, Nat Comms. 13: 476. https://doi.org/10.1038/s41467-022-27967-9.. Kišonaitė, M., Wild, K., Lapouge, K., Ruppert, T. & Sinning, I. (2022)
HYPK promotes the activity of the Nα-acetyltransferase A complex to determine proteostasis of nonAc-X2/N-degron-containing proteins, Sci. Adv. 8:eabn6153. doi: https://doi.org/10.1126/sciadv.abn6153. Miklánková, P., Linster, E., Boyer, J.B., Weidenhausen, J., Mueller, J., Armbruster, L., Lapouge, K., De La Torre, C., Bienvenut, W., Sticht, C., Mann, M., Meinnel, T., Sinning, I., Giglione, C., Hell, R. & Wirtz, M. (2022)
The inner nuclear membrane protein Lem2 coordinates RNA degradation at the nuclear periphery. Nat Struct Mol Biol. 2022 Sep;29(9):910-921. doi: 10.1038/s41594-022-00831-6. Epub 2022 Sep 19. PMID: 36123402; PMCID: PMC9507967. Caballero, L.M., Capella, M., Barrales, R.R., Dobrev, N., van Emden, T., Fischer-Burkart, S., Kinugasa, Y., Hirano, Y., Sinning, I., Fischer, T., Hiraoka, Y. & Braun, S. (2022)
SRP54 mutations induce congenital neutropenia via dominant-negative effects on XBP1 splicing. Blood, 137(10), 1340–1352. https://doi.org/10.1182/blood.2020008115 Schürch, C., Schaefer, T., Müller, J. S., Hanns, P., Arnone, M., Dumlin, A., Schärer, J., Sinning, I., Wild, K., Skokowa, J., Welte, K., Carapito, R., Bahram, S., Konantz, M., & Lengerke, C. (2021)
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Commun Biol 4, 600. https://doi.org/10.1038/s42003-021-02132-y Soni, K., Kempf, G., Manalastas-Cantos, K., Hendricks, A., Flemming, D., Guizetti, J., Simon, B., Frischknecht, F., Svergun, D.I., Wild, K., & Sinning, I. (2021)
Structural and functional characterization of the N-terminal acetyltransferase Naa50. Structure, 29(5), 413–425.e5. https://doi.org/10.1016/j.str.2020.12.004 Weidenhausen, J., Kopp, J., Armbruster, L., Wirtz, M., Lapouge, K., & Sinning, I. (2021)
Structural and functional impact of SRP54 mutations causing severe congenital neutropenia. Structure, 29. doi: http://doi.org/10.1016/j.str.2020.09.008 Juaire, K.D., Lapouge, K., Becker, M.M.M., Kotova, I., Michelhans, M., Carapito, R., Wild, K., Bahram, S. & Sinning, I. (2021)
Structural and molecular mechanisms for membrane protein biogenesis by the Oxa1 superfamily. Nat Struct Mol Biol 28, 234–239. https://doi.org/10.1038/s41594-021-00567-9 McDowell, M.A., Heimes, M. & Sinning, I. (2021)
Structural basis of Naa20 activity towards a canonical NatB substrate. Commun Biol 4, 2. https://doi.org/10.1038/s42003-020-01546-4 Layer, D., Kopp, J., Fontanillo, M., Köhn, M., Lapouge, K. & Sinning, I. (2021)
The zinc-finger protein Red1 orchestrates MTREC submodules and binds the Mtl1 helicase arch domain. Nat Comms. 12: 3456. PMID: 34103492. doi: https://doi.org/10.1038/s41467-021-23565-3 Dobrev, N., Ahmed, Y.L., Sivadas, A., Fischer*, T. & Sinning*, I. (2021)
Cholesterol localization around the metabotropic glutamate receptor 2, J. Phys. Chem. B 24: 9061-9078. PMID: 32954729. Kurth, M., Lolicato, F., Sandoval-Perez, A., Amaya-Espinosa, H., Teslenko, A., Sinning, I., Beck, R., Brügger B. & Aponte-Santamaria, C.A. (2020)
Complexin suppresses spontaneous exocytosis by capturing the membrane-proximal regions of VAMP2 and SNAP25. Cell Reports, 32. https://doi.org/10.1016/j.celrep.2020.107926 Malsam, J., Bärfuss, S., Trimbuch, T.h, Zarebidaki, F., Sonnen, A., Wild, K., Scheutzow, A., Rohland, L., Mayer, M., Sinning, I., Briggs, J., Rosenmund, C. & Söllner, T.H. (2020)
Functional implications of MIR domains in protein O-mannosylation, eLife 9: e61189. PMID: 33357379.
Chiapparino#, A., Grbavac#, A., Jonker, H.R.A., Hackmann, Y., Mortensen, S., Zatorska, E., Schott, A., Stier, G., Saxena, K., Wild, K., Schwalbe, H., Sabine Strahl*, S. & Sinning*, I. (2020)
MetAP-like Ebp1 occupies the human ribosomal tunnel exit and recruits flexible rRNA expansion segments, Nat Comms. 11: 776. PMID: 32034140.
Wild, K., Aleksić, M., Lapouge, K., Juaire, K.D., Flemming, D., Pfeffer, S. & Sinning, I. (2020)
NAA50 is an enzymatically active Nα-acetyltransferase that is crucial for the development and regulation of stress responses, Plant Physiol. 183: 1502-1516.
Armbruster, L., Linster, E., Boyer, J.B., Brünje, A., Eirich, J., Stephan, I., Bienvenut, W.V., Weidenhausen, J., Meinnel, T., Hell, R., Sinning, I., Finkemeier, I., Giglione,G. & Wirtz, M. (2020)
N-terminal acetylation by NatB affects growth and abiotic stress responses in Arabidopsis, Plant Physiol. 182: 792-806. PMID: 31744933.
Huber, M., Bienvenut, W.V., Linster, E., Stephan, I., Armbruster, L., Sticht, C., Layer, D., Lapouge, K., Meinnel, T., Sinning, I., Giglione, C., Hell, R. & Wirtz, M. (2020)
Structural basis for the complex DNA binding behaviour of the plant stem cell regulator WUSCHEL, Nat. Comms. 11: 2223. PMID: 32376862.
Sloan, J., Hakenjos, J.P., Gebert, M., Ermakova, O., Gumiero, A., Stier, G., Wild, K., Sinning*, I. & Lohmann*, J.U. (2020)
Structural basis of tail-anchored membrane protein biogenesis by the GET insertase complex, Mol Cell 80: 72-86.e7. PMID: 32910895.
McDowell*, M.A., Heimes, M., Fiorentino, F., Mehmood, S., Farkas, Á., Coy-Vergara, J., Wu, D., Schmid, V., Heinze, R., Reddy Bolla, J., Wild, K., Flemming, D., Pfeffer, S., Schwappach, B., Robinson, C.V. & Sinning*, I. (2020)
The Arabidopsis Nα-acetyltransferase NAA60 locates to the plasma membrane and is vital for the high salt stress response, New Phytologist, doi: 10.1111/nph.16747. Online ahead of print. PMID: 32548857
Linster#, E., Layer#, D., Bienvenut, W.V., Dinh-Van, T., Weyer, F., Lemhuis, W., Brünje, A., Hoffrichter, M., Miklankova, P., Sindlinger, J., Schwarzer, D., Kopp, J., Lapouge, K., Meinnel, T., Giglione, C., Finkemeier, I., Hell, R., Sinning*, I. & Wirtz*, M. (2020)
The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb, Nat Comms. 11: 1504. PMID: 32198371.
Zhang*, Y., Valentín Gesé*, G., Conz, C., Lapouge, L., Kopp, J., Wölfle, T., Rospert, S. & Sinning, I. (2020)
Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin–ligand-type complexes. Nat Commun 10, 3050. https://doi.org/10.1038/s41467-019-10922-6 Ahmed, Y.L., Thoms, M., Mitterer, V., Sinning, I., & Hurt, E. (2019)
Identification of YvcI as novel RNA pyrophospho-hydrolase from B. subtilis, J. Biol. Chem. 94: 19967-19977. PMID: 31740579.
Frindert, J., Kahloon, M.A., Zhang, Y., Ahmed, Y.L., Sinning, I., & Jäschke, A. (2019)
Novel variants and clinical symptoms in four new ALG3-CDG patients, review of the literature, and identification of AAGRP-ALG3 as a novel ALG3 variant with alanine and glycine-rich N-terminus. Hum Mutat. 40: 938-951. PMID: 31067009.
Himmelreich N, Dimitrov B, Geiger V, Zielonka M, Hutter AM, Beedgen L, Hüllen A, Breuer M, Peters V, Thiemann KC, Hoffmann GF, Sinning I, Dupré T, Vuillaumier-Barrot S, Barrey C, Denecke J, Kölfen W, Düker G, Ganschow R, Lentze MJ, Moore S, Seta N, Ziegler A, Thiel C. (2019)
Reconstitution of the human SRP system and quantitative and systematic analysis of its ribosome interactions, Nucl. Acids Res. 47: 3184-3196.
Wild, K., D. Juaire, K.D., Soni, K., Shanmuganathan, V., Hendriks, A., Segnitz, B., Beckmann, R. & Sinning, I. (2019)
Structure, dynamics, and interactions of large SRP variants (review), Biol. Chem. 401: 63-80. PMID: 31408431.
Wild, K., Becker, MMM, Kempf, G. & Sinning, I. (2019)
DENR-MCTS1 heterodimerization and tRNA recruitment are required for translation reinitiation. PLoS Biol. 16: e2005160. PMID: 29889857.
Ahmed, Y.L., Schleich, S., Bohlen, J., Mandel, N., Simon, B., Sinning*, I. & Teleman*, A.A. (2018)
The Escherichia coli SRP receptor forms a homodimer at the membrane, Structure 26:1440-1450.e5. PMID: 30146170.
Kempf, G., Stjepanovic, G., Hendricks, A., Lapouge, K., & Sinning, I. (2018)
9Å structure of COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments, Elife 6. pii: e26691. Dodonova, S.O., Aderhold, P., Kopp, J., Ganeva, I., Röhling, S., Hagen, W.J.H., Sinning, I., Wieland, F., & Briggs, J.A.G. (2017)
Accumulation of phosphatidylcholine on gut intestinal mucosa surface is not dominated by electrostatic interactions, BBA Biomembranes 1859: 959-965.
Korytowski, A., Abuillan, W., Amadei, F., Makky, A., Gumiero, A., Sinning, I., Gauss, A., Stremmel, W. & Tanaka, M. (2017)
Fe65-PTB2 dimerization mimics Fe65-APP interaction, Front. Mol Neurosci. 10: 140.
Feilen, L.P., Haubrich, K., Strecker, P., Probst, S., Eggert, S., Stier, G., Sinning, I., Konietzko, U., Kins, S., Simon, B. & Wild, K. (2017)
Interaction network of the ribosome assembly machinery from a eukaryotic thermophile. Protein science 26(2), 327–342. https://doi.org/10.1002/pro.3085 Baßler, J., Ahmed, Y.L., Kallas, M., Kornprobst, M., Rodriguez-Calvino, F., Gnädig, M., Thoms, M., Stier, G., Ismail, S., Kharde, S., Castillo, N., Griesel, S., Bastuck, S., Bradatsch, B., Thomson, E., Flemming, D., Sinning, I.* & Hurt, E.* (2017)
Lysine relay mechanism coordinates intermediate transfer in vitamin B6 biosynthesis, Nat. Chem. Biol. 3: 290-294.
Rodrigues, M.J., Windeisen, V., Zhang,Y., Guédez,G., Weber, S., Strohmeier, M., Hanes, J.W., Royant, A., Evans, G., Sinning, I., Ealick, S.E., Begley, T.P. & Tews, I. (2017)
Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome, PlosOne 12: e0183272. Sá-Moura, B., Kornprobst, M., Kharde, S., Ahmed, Y.L., Stier, G., Kunze, R., Sinning*, I. & Hurt*, E. (2017)
Structural basis for 5'-ETS recognition by Utp4 at the early stages of ribosome biogenesis. PLOS ONE 12(6): e0178752. https://doi.org/10.1371/journal.pone.0178752 Calviño, F.R., Kornprobst, M., Schermann, G., Birkle, F., Wild, K., Fischer, T., Hurt, E., Ahmed, Y.L. & Sinning, I. (2017)
Structural basis of HypK regulating N-terminal acetylation by the NatA complex, Nat Comms 8: 15726.
Weyer, F.A., Gumiero, A., Lapouge, K., Bange, G., Kopp, J. & Sinning, I. (2017)
Structural insights into a unique Hsp70/Hsp40 interaction in the eukaryotic ribosome-associated complex, Nat. Struct. Mol. Biol. 24:144-151.
Weyer, F. A., Gumiero, A., Valentín Gesé, G., Lapouge, K. & Sinning, I. (2017)
Structures of human SRP72 reveal its function in co-translational protein targeting, Nucl. Acids Res. 45: 470-481.
Becker, M.M.M., Lapouge, K., Segnitz, B., Wild, K. & Sinning, I. (2017)
Two chaperones locked in an embrace: Structure and function of the ribosome-associated complex RAC, Nat. Struct. Mol. Biol. 24: 611-619.
Zhang, Y., Sinning, I. & Rospert, S. (2017)
Visualizing the assembly pathway of nucleolar pre-60S ribosomes, Cell 171: 1599-1610. Kater, L., Thoms, M., Barrio Garcia, C., Cheng, J., Ismail, S., Ahmed, Y.L., Bange, G., Kressler, D., Berninghausen, O., Sinning, I., Hurt, E. & Beckmann, R. (2017)
Visualizing the earliest steps during nucleolar pre-60S ribosome assembly. Cell 171, 1599–1610. Lukas Kater, Matthias Thoms, Clara Barrio Garcia, Jingdong Cheng, Sherif Ismail, Yasar Luqman Ahmed, Gert Bange, Dieter Kressler, Otto Berninghausen, Irmi Sinning, Ed Hurt and Roland Beckmann (2017)
Concerted removal of the Erb1-Ytm1 complex in ribosome biogenesis relies on an elaborate interface, Nucl. Acids Res. 44: 926-39. Thoms, M., Ahmed. Y.L., Maddi, K., Hurt, E. & Sinning, I. (2016)
Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain, Nat. Comms. 7: 13563. Gumiero, A., Conz, C., Valentín Gesé, G., Zhang, Y., Weyer, F. A., Lapouge, K., Kappes, J., von Plehwe, U., Schermann, G., Fitzke, E., Wölfle, T., Fischer, T., Rospert, S. & Sinning, I. (2016)
RNA-DNA hybrids and RNase H activity are required for efficient DSB repair, Cell 167: 1001-13. Ohle, C., Tesorero, R., Schermann, G., Dobrev, N., Sinning, I. & Fischer, T. (2016)
Structural basis for conserved regulation and adaptation of the signal recognition particle targeting complex, J. Mol. Biol. 428: 2880-97.
Wild, K., Bange, G., Motiejunas, D., Kribelbauer, J., Hendricks, A., Segnitz, B., Wade, R., & Sinning, I. (2016)
A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation, J. Cell Biol. 210: 169-70. Bassler, J., Paternoga, H., Holdermann, I., Thoms, M., Grannemann, S., Barrio-Garcia, C., Nyarko, A., Lee, W. Stier, G., Clark, S., Schraivogel, D., Kallas, M., Beckmann, R., Tollervey, D., Barbar, E., Sinning*, I. & Hurt*, E. (2015)
Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones. Nature communications, 6, 7494. https://doi.org/10.1038/ncomms8494 Pausch, P., Singh, U., Ahmed, Y. L., Pillet, B., Murat, G., Altegoer, F., Stier, G., Thoms, M., Hurt, E., Sinning, I., Bange, G., & Kressler, D. (2015)
Expression of membrane proteins in the eyes of transgenic Drosophila melanogaster. Methods Enzymol. 556: 219-39. Hackmann, Y., Jödicke, L., Panneels, V. & Sinning, I. (2015)
Formation of Disulfide Bridges Drives oligomerization, membrane pore formation and translocation of fibroblast growth factor 2 to cell surfaces, J. Biol. Chem. 290: 8925-37. Müller, H.M., Steringer, J.S., Wegehingel, S., Bleicken, S., Münster, M., Dimou, E., Unger, S., Weidmann, G., Andreas H., Garcia-Saez, A., Wild, K., Sinning, I. & Nickel, W. (2015)
Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocation, Nat Comms. 6: 10133.
Jadhav, B., McKenna, M., Johnson, N., High, S., Sinning, I. & Pool, M.R. (2015)
Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction, Nat Comms. 6: 8875.
Horn, A., Hennig, J., Ahmed, J.L., Stier, G., Wild, K., Sattler, M. & Sinning, I. (2015)
Structure and switch cycle of SRβ as ancestral eukaryotic GTPase associated with secretory membranes, Structure 23: 1838-47.
Jadhav, B., Wild, K., Pool, M.R. & Sinning, I. (2015)
Strukturelle Evolution des Signalerkennungspartikels, Biospektrum 02: 161-163.
Kempf, G., Wild, K. & Sinning, I. (2015)
Symportin 1 chaperones 5S RNP assembly during ribosome biogenesis by occupying an essential rRNA-binding site. Nat Commun 6, 6510. https://doi.org/10.1038/ncomms7510 Calviño, F.R., Kharde, S., Ori, A., Hendricks, A., Wild, K., Kressler, D., Bange, G., Hurt, E., Beck, M. & Sinning, I. (2015)
The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis, Nucl. Acids Res. 43: 7083-95.
Kharde, S., Calviño, F.R., Gumiero, A., Wild, K. & Sinning, I. (2015)
Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions, Nat. Struct. Mol. Biol. 22: 767-73.
Beckert, B., Kedrov, A., Sohmen, D., Kempf, G., Wild, K., Sinning, I., Stahlberg, H., Wilson, D. & Beckmann, R. (2015)
60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein particle, Nat. Commun. 5: 3491. doi: 10.1038/ncomms4491. Leidig, C., Thoms, M., Holdermann, I., Bradatsch, B., Berninghausen, O., Bange, G., Sinning, I., Hurt, E. & Beckmann, R. (2014)
A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation, J. Cell Biol. 207: 481-498. Bassler, J., Paternoga, H., Holdermann, I., Thoms, M., Grannemann, S., Barrio-Garcia, C., Nyarko, A., Stier, G., Clark, S., Schraivogel, D., Kallas, M., Beckmann, R., Tollervey, D., Barbar, E., Sinning*, I. & Hurt*, E. (2014)
An Extended Helical Conformation in Domain 3a of Munc18-1 Provides a Template for SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Complex Assembly. J.Biol.Chem. 289, 9639-9650. https://doi.org/10.1074/jbc.M113.514273 Parisotto, D., Pfau, M., Scheutzow, A., Wild, K., Mayer, M.P., Malsam, J., Sinning, I., & Söllner, T.H. (2014)
Longin and GAF Domains: Structural Evolution and Adaptation to the Subcellular Trafficking Machinery. Traffic 15: 104-21.
De Franceschi, N., Wild, K., Schlacht, A., Dacks, J.B., Sinning, I. & Filippini, F. (2014)
RNA gymnastics in mammalian signal recognition particle assembly, RNA Biol. 11: 1330-1334.
Wild, K. & Sinning, I. (2014)
SRP RNA remodeling by SRP68 explains its role in protein translocation, Science 344: 101-104. DOI:10.1126/science.1249094.
Grotwinkel, J.T., Wild, K., Segnitz, B. & Sinning, I. (2014)
Structure of the tRNA-like bacterial Alu domain Nucl. Acids Res. 42: 12284-94.
Kempf, G., Wild, K. & Sinning, I. (2014)
Consistent mutational paths predict eukaryotic thermostability. BMC evolutionary biology, 13, 7. https://doi.org/10.1186/1471-2148-13-7 van Noort, V., Bradatsch, B., Arumugam, M., Amlacher, S., Bange, G., Creevey, C., Falk, S., Mende, D. R., Sinning, I., Hurt, E., & Bork, P. (2013)
Endoplasmic reticulum Targeting and Insertion of Tail-anchored membrane proteins by the GET pathway. Cold Spring Harb Perspect Biol. 5(8). doi:pii: a013334.
Denic, V., Doetsch, V. & Sinning, I. (2013)
New twist to nuclear import: When two travel together, Com. & Int. Biol. 6:4, e24792; July/August 2013, Landes Bioscience). Bange, G. , Murat, G., Sinning, I., Hurt, E. & Kressler, D. (2013)
SIMIBI Twins in protein targeting and localization, Nat. Struct. Mol. Biol. 20:776-80. doi: 10.1038/nsmb.2605.
Bange, G. & Sinning, I. (2013)
Structural characterization of a eukaryotic co-translational chaperone, the ribosome-associated complex (RAC), Nat. Struct. Mol. Biol. 20:23-8. Leidig, C., Bange, G., Kopp, J., Amlacher, S., Aravind, A., Wickles, S., Witte, G., Hurt, E., Beckmann, R. & Sinning, I. (2013)
Assembly of the eukaryotic PLP-synthase complex from Plasmodium and activation of the Pdx1 enzyme, Structure 20:172-84.
Guédez, G., Hipp, K., Windeisen, V., Derrer, B., Gengenbacher, M., Böttcher, B., Sinning, I., Kappes, B. & Tews, I. (2012)
Chromodomains read the arginine code of post-translational targeting, Nat. Struct. Mol. Biol. 19: 260-3.
Holdermann, I., Meyer, H., Round, A., Wild, K., Sattler, M. & Sinning, I. (2012)
Structure and conservation of the periplasmic targeting factor tic22 protein from plants and cyanobacteria, J. Biol. Chem. 287: 24164-73.
Tripp, J., Hahn, A., Koenig, P., Flinner, N., Bublak, D., Ertel, F., Brouwer, E.M., Mirus, O., Sinning, I., Tews, I. & Schleiff, E. (2012)
Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones, Mol Cell, 2012 Nov 1. doi:pii: S1097-2765(12)00823-4. 10.1016/j.molcel.2012.09.023.
Kityk, R., Kopp, J., Sinning, I. & Mayer, M.P. (2012)
Synchronizing nuclear import of ribosomal proteins with ribosome assembly, Science 338: 666-71. Kressler*, D., Bange, G. Ogawa, Y., Bradatsch, B., Pratte, D., Strauß, D., Amlacher, S., Yoneda,Y., Katahira, J., Sinning, I.*, & Hurt, E.* (2012)
Binding of chloroplast signal recognition particle to a thylakoid membrane protein substrate in aqueous solution and delineation of the cpSRP43-substrate interaction domain. Biochem J. 437(1):149-55.
Cain P, Holdermann I, Sinning I, Johnson AE, Robinson C. (2011)
Drosophila photoreceptor cells exploited for the production of eukaryotic membrane proteins: receptors, transporters and channels. PLoS One. 6(4):e18478.
Panneels V, Kock I, Krijnse-Locker J, Rezgaoui M, Sinning I. (2011)
It takes two to Get3. Structure. 19(10):1353-55. Sinning, I., Bange, G. & Wild, K. (2011)
Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targeting. J Biol Chem. 286(26):23489-97. Epub 2011 May 3.
Stjepanovic G, Kapp K, Bange G, Graf C, Parlitz R, Wild K, Mayer MP, Sinning I. (2011)
Mdm38 is a 14-3-3-Like Receptor and Associates with the Protein Synthesis Machinery at the Inner Mitochondrial Membrane. Traffic. 12 (10):1457-66.
Lupo D, Vollmer C, Deckers M, Mick DU, Tews I, Sinning I, Rehling P. (2011)
Molecular Basis for the Unique Role of the AAA+ Chaperone ClpV in Type VI Protein Secretion. J Biol Chem. 286(34):30010-21.
Pietrosiuk A, Lenherr ED, Falk S, Bönemann G, Kopp J, Zentgraf H, Sinning I, Mogk A. (2011)
Phosphorylation of LRP1 regulates the interaction with Fe65. FEBS Lett. 585:3229-35.
Klug W, Dietl A, Simon B, Sinning I, Wild K. (2011)
Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex. Science. 333(6043):758-62.
Stefer S, Reitz S, Wang F, Wild K, Pang YY, Schwarz D, Bomke J, Hein C, Löhr F, Bernhard F, Denic V, Dötsch V, Sinning I. (2011)
Structural basis for the molecular evolution of SRP-GTPase activation by protein. Nat Struct Mol Biol. 8:1376-80. Bange G, Kümmerer N, Grudnik P, Lindner R, Petzold G, Kressler D, Hurt E, Wild K, Sinning I. (2011)
Substrate binding disrupts dimerization and induces nucleotide exchange of the chloroplast GTPase Toc33. Biochem J. 436(2):313-9.
Oreb M, Höfle A, Koenig P, Sommer MS, Sinning I, Wang F, Tews I, Schnell DJ, Schleiff E. (2011)
Arabidopsis stromal-derived Factor2 (SDF2) is a crucial target of the unfolded protein response in the endoplasmic reticulum. J Biol Chem. 285(23):18113-21.
Schott A, Ravaud S, Keller S, Radzimanowski J, Viotti C, Hillmer S, Sinning I, Strahl S. (2010)
Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of SDF2-like protein from Arabidopsis thaliana. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66(Pt 1):12-4.
Radzimanowski J, Ravaud S, Schott A, Strahl S, Sinning I. (2010)
Conserved properties of polypeptide transport-associated (POTRA) domains derived from cyanobacterial Omp85. J Biol Chem. 285(23):18016-24.
König P, Mirus O, Haarmann R, Sommer MS, Sinning I, Schleiff E, Tews I. (2010)
cpSRP43 is a novel chaperone specific for light-harvesting chlorophyll a,b-binding proteins. J Biol Chem. 285(28):21655-61.
Falk S, Sinning I. (2010)
Defining the structural requirements for ribose 5-phosphate-binding and intersubunit cross-talk of the malarial pyridoxal 5-phosphate synthase. FEBS Lett. 584(19):4169-74.
Derrer B, Windeisen V, Guédez Rodríguez G, Seidler J, Gengenbacher M, Lehmann WD, Rippe K, Sinning I, Tews I, Kappes B. (2010)
FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system. Proc Natl Acad Sci U S A. 107(25):11295-300.
Bange G, Kümmerer N, Engel C, Bozkurt G, Wild K, Sinning I. (2010)
Genetic evidence for functional interaction of the Escherichia coli signal recognition particle receptor with acidic lipids in vivo. J Biol Chem. 285(52):40508-14. Erez E, Stjepanovic G, Zelazny AM, Brügger B, Sinning I, Bibi E. (2010)
Membrane protein expression in the eyes of transgenic flies. Methods Mol Biol. 601:135-47.
Panneels V, Sinning I. (2010)
Signal peptide peptidase (SPP) assembles with substrates and misfolded membrane proteins into distinct oligomeric complexes. Biochem J. 427(3):523-34.
Schrul B, Kapp K, Sinning I, Dobberstein B. (2010)
Structural insights into the assembly of the human and archaeal signal recognition particles. Acta Crystallogr D Biol Crystallogr. 66(Pt 3):295-303.
Wild K, Bange G, Bozkurt G, Segnitz B, Hendricks A, Sinning I. (2010)
The C terminus of Alb3 interacts with the chromodomains 2 and 3 of cpSRP43. J Biol Chem. 285(53):le25-6;
Falk S, Sinning I. (2010)
The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane. J Biol Chem. 285(8):5954-62.
Falk S, Ravaud S, Koch J, Sinning I. (2010)
The structure of Get4 reveals an alpha-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesis. FEBS Lett. 584(8):1509-14. Bozkurt G, Wild K, Amlacher S, Hurt E, Dobberstein B, Sinning I. (2010)
Delivering proteins for export from the cytosol. Nat Rev Mol Cell Biol. 10(4):255-64. Review.
Cross BC, Sinning I, Luirink J, High S. (2009)
Dissection of contributions from invariant amino acids to complex formation and catalysis in the heteromeric pyridoxal 5-phosphate synthase complex from Bacillus subtilis. Biochemistry. 48(9):1928-35.
Wallner S, Neuwirth M, Flicker K, Tews I, Macheroux P. (2009)
Protein targeting by the signal recognition particle. Biol Chem. 390(8):775-82. Review.
Grudnik P, Bange G, Sinning I. (2009)
Signal sequences get active. Nat Chem Biol. 5(3):146-7.
Sinning I, Wild K, Bange G. (2009)
Structural insights into tail-anchored protein binding and membrane insertion by Get3. Proc Natl Acad Sci U S A. 106(50):21131-6. Bozkurt G, Stjepanovic G, Vilardi F, Amlacher S, Wild K, Bange G, Favaloro V, Rippe K, Hurt E, Dobberstein B, Sinning I. (2009)
Targeting of Drosophila rhodopsin requires helix 8 but not the distal C-terminus. PLoS One. 4(7):e6101.
Kock I, Bulgakova NA, Knust E, Sinning I, Panneels V. (2009)
X-ray crystal structure of Saccharomyces cerevisiae Pdx1 provides insights into the oligomeric nature of PLP synthases. FEBS Lett. 583(13):2179-86.
Neuwirth M, Strohmeier M, Windeisen V, Wallner S, Deller S, Rippe K, Sinning I, Macheroux P, Tews I. (2009)
Crystal structure of the human Fe65-PTB1 domain. J Biol Chem. 283(34):23113-20.
Radzimanowski J, Ravaud S, Schlesinger S, Koch J, Beyreuther K, Sinning I, Wild K. (2008)
Membrane curvature induced by Arf1-GTP is essential for vesicle formation. Proc Natl Acad Sci U S A 105, 11731-11736. → Highlighted by the Faculty of 1000 (F1000.com/1119165). http://www.pnas.org/content/105/33/11731 Beck, R, Sun, Z, Adolf, F, Rutz, C, Bassler, J, Wild, K, Sinning, I, Hurt, E, Brügger, B, Béthune, J*, and Wieland, F* (2008)
Mercury-induced crystallization and SAD phasing of the human Fe65-PTB1 domain. Acta Crystallogr Sect F Struct Biol Cryst Commun. 64(Pt 5):382-5.
Radzimanowski J, Ravaud S, Beyreuther K, Sinning I, Wild K. (2008)
On the significance of Toc-GTPase homodimers. J Biol Chem. 283(34):23104-12.
König P, Oreb M, Rippe K, Muhle-Goll C, Sinning I, Schleiff E, Tews I. (2008)
Overproduction, purification, crystallization and preliminary X-ray analysis of human Fe65-PTB2 in complex with the amyloid precursor protein intracellular domain. Acta Crystallogr Sect F Struct Biol Cryst Commun. 64(Pt 5):409-12.
Radzimanowski J, Beyreuther K, Sinning I, Wild K. (2008)
pH Sensitivity of the GTPase Toc33 as a regulatory circuit for protein translocation into chloroplasts. Plant Cell Physiol. 49(12):1917-21.
Bionda T, König P, Oreb M, Tews I, Schleiff E. (2008)
Policing Tic 'n' Toc, the doorway to chloroplasts. Trends Cell Biol. 18(1):19-27. Review.
Oreb M, Tews I, Schleiff E. (2008)
Purification, crystallization and preliminary structural characterization of the periplasmic domain P1 of the Escherichia coli membrane-protein insertase YidC. Acta Crystallogr Sect F Struct Biol Cryst Commun. 64(Pt 2):144-8.
Ravaud S, Wild K, Sinning I. (2008)
Structural basis for a distinct catalytic mechanism in Trypanosoma brucei tryparedoxin peroxidase. J Biol Chem. 283(44):30401-11. Melchers J, Diechtierow M, Fehér K, Sinning I, Tews I, Krauth-Siegel RL, Muhle-Goll C. (2008)
Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43. Science. 321(5886):253-6.
Stengel KF, Holdermann I, Cain P, Robinson C, Wild K, Sinning I. (2008)
Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2. EMBO Rep. 9(11):1134-40.
Radzimanowski J, Simon B, Sattler M, Beyreuther K, Sinning I, Wild K. (2008)
The crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleft. J Biol Chem. 283(14):9350-8.
Ravaud S, Stjepanovic G, Wild K, Sinning I. (2008)
The GTPase cycle of the chloroplast import receptors Toc33/Toc34: implications from monomeric and dimeric structures. Structure. 16(4):585-96.
König P, Oreb M, Höfle A, Kaltofen S, Rippe K, Sinning I, Schleiff E, Tews I. (2008)
Arx1 functions as an unorthodox nuclear export receptor for the 60S pre-ribosomal subunit, Molecular Cell 27:767-79.
Bradatsch B, Katahira J, Kowalinski E, Bange G, Yao W, Sekimoto T, Baumgärtel V, Boese G, Bassler J, Wild K, Peters R, Yoneda Y, Sinning I, Hurt E. (2007)
Canonical Signal Recognition Particle Components Can Be Bypassed for Posttranslational Protein Targeting in Chloroplasts. Plant Cell 19:1635-48.
Tzvetkova-Chevolleau T, Hutin C, Noël LD, Goforth R, Carde JP, Caffarri S, Sinning I, Groves M, Teulon JM, Hoffman NE, Henry R, Havaux M, Nussaume L. (2007)
E. coli SRP-receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix. J. Biol. Chem. 282:32176-184.
Parlitz R, Eitan A, Stjepanovic G, Bahari L, Bange G, Bibi E, Sinning I. (2007)
Expression, purification and preliminary crystallographic characterization of FlhF from Bacillus subtilis, Acta Cryst F. 63: 449-451.
Bange G, Petzold G, Wild K, Sinning I. (2007)
Expression, purification, crystallization and preliminary crystallographic analysis of the proliferation associated protein Ebp1. Acta Cryst F 63: 768-770.
Kowalinski E, Bange G, Wild K, Sinning I. (2007)
Functional analysis of PDX2 from Arabidopsis, a glutaminase involved in vitamin B6 biosynthesis. Plant Physiol. 144:915-25.
Tambasco-Studart M, Tews I, Amrhein N, Fitzpatrick TB. (2007)
Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY. J. Biol. Chem. 282:32168-175.
Bahari L, Parlitz R, Eitan A, Stjepanovic G, Bochkareva ES, Sinning I, Bibi E. (2007)
Protein translocation: Checkpoint role for SRP GTPase activation. Curr. Biol. 17:R980-R982.
Bange G, Wild K, Sinning I. (2007)
Structural and Thermodynamic Insights into the Assembly of the Heteromeric Pyridoxal Phosphate Synthase from Plasmodium falciparum. J Mol Biol. 374:732-48.
Flicker K, Neuwirth M, Strohmeier M, Kappes B, Tews I, Macheroux P. (2007)
The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis. Dev Cell. 12:739-50.
Peplowska K, Markgraf DF, Ostrowicz CW, Bange G, Ungermann C. (2007)
The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions. FEBS Letters 581: 4450-4454.
Kowalinski E, Bange G, Bradatsch B, Hurt E, Wild K, Sinning I. (2007)
The crystal structure of the third SRP GTPase FlhF reveals a homodimer with bound GTP. Proc. Natl. Acad.Sci. USA 104: 13621-13625.
Bange G, Petzold G, Wild K, Parlitz RO, Sinning I. (2007)
The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site. FEBS Letters 581:5671-6.
Stengel KF, Holdermann I, Wild K, Sinning I. (2007)
The structure of the regulatory domain of the adenylyl cyclase Rv1264 from Mycobacterium tuberculosis with bound oleic acid. J. Mol. Biol. 369:1282-95.
Findeisen F, Linder JU, Schultz A, Schultz JE, Brügger B, Wieland F, Sinning I, Tews I. (2007)
Thermodynamic characterization of the protein-protein interaction in the heteromeric Bacillus subtilis pyridoxalphosphate synthase. Biochemistry 46:5131-9.
Neuwirth M, Flicker K, Strohmeier M, Tews I, Macheroux P. (2007)
Two independent routes of de novo vitamin B6 biosynthesis: not that different after all. Biochem J. 407:1-13.
Fitzpatrick TB, Amrhein N, Kappes B, Macheroux P, Tews I, Raschle T. (2007)
Fatty acid regulation of adenylyl cyclase Rv2212 from Mycobacterium tuberculosis H37Rv. FEBS J. 273(18):4219-28.
Motaal A, Tews I, Schultz JE, Linder JU. (2006)
Following the signal sequence from ribosomal tunnel exit to signal recognition particle. Nature. 444(7118):507-11.
Halic M, Blau M, Becker T, Mielke T, Pool MR, Wild K, Sinning I, Beckmann R. (2006)
Signal recognition particle receptor exposes the ribosomal translocon binding site. Science. 312(5774):745-7.
Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, Sinning I, Beckmann R. (2006)
Structure of a bacterial pyridoxal 5'-phosphate synthase complex. Proc Natl Acad Sci U S A. 103(51):19284-9.
Strohmeier M, Raschle T, Mazurkiewicz J, Rippe K, Sinning I, Fitzpatrick TB, Tews I. (2006)
The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64. EMBO J. 25(9):1836-47.
Qbadou S, Becker T, Mirus O, Tews I, Soll J, Schleiff E. (2006)
The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains. J Biol Chem. 281(13):8898-906.
Schlenker O, Hendricks A, Sinning I, Wild K. (2006)
Vitamin B6 biosynthesis by the malaria parasite Plasmodium falciparum: Biochemical and structural insights. J Biol Chem. 281(6):3633-41.
Gengenbacher M, Fitzpatrick TB, Raschle T, Flicker K, Sinning I, Müller S, Macheroux P, Tews I, Kappes B. (2006)
The structure of a pH sensing mycobacterial adenylyl cyclase holoenzyme, Science 308: 1020-1023.
Tews, I., Findeisen, F., Sinning, I., Schultz A., Schultz, J.E. & Linder, J.U. (2005)
A structural step into the SRP cycle, Mol. Microbiol. 53: 357-63.
Wild, K., Rosendal, K. & Sinning, I. (2004)
Co-translational protein targeting: SRP meets the ribosome, Nat. Struct. Mol. Biol. 11: 1049-53.
Wild, K., Halic, M., Sinning, I. & Beckmann, R. (2004)
Crystallization and preliminary X-ray diffraction studies of the crenarchaeal SRP core, Acta Cryst. D60: 140-143.
Rosendal, K.R., Sinning, I. & Wild, K. (2004)
Crystallization of a Golgi-associated PR-1 related protein (GAPR-1) that localizes to lipid-enriched microdomains, Acta Cryst. D60: 730–732.
Groves, M.R., Kuhn, A., Hendricks, A., Radke, S., Serrano, R.L., Helms, J.B & Sinning, I. (2004)
Signal recognition particle mediates posttranslational targeting in eukaryotes, EMBO J. 23:2755-64.
Abell. B., Pool., M., Schlenker, O., Sinning, I. & High, S. (2004)
SRP-mediated protein targeting: structure and function revisited, BBA Mol. Cell Res. 1694: 17-35.
Luirink, J. & Sinning, I. (2004)
Structural analysis of the human Golgi-associated plant pathogenesis related protein GAPR-1 implicates dimerization as a regulatory mechanism, J. Mol. Biol. 339: 173-83.
Serrano, R.L., Kuhn, A., Hendricks, A., Helms, J.B., Sinning, I. & Groves, M.R. (2004)
Structural biology. Surprising news from the PCC. Science 303: 320-2.
Dobberstein, B. & Sinning. I. (2004)
Choline head groups stabilize the matrix loop regions of the ATP/ADP carrier ScAAC2. Biochem. Biophys. Res. Com. 300: 65-74.
Panneels, V., Schüssler, U., Costagliola, S. & Sinning, I. (2003)
Crystal structure of the complete core of archaeal signal recognition particle and implications for inter-domain communication, Proc. Natl. Acad. Sci. USA 100: 14701-14706.
Rosendal, K.R., Wild, K., Montoya, G. & Sinning, I. (2003)
Definition of Domain Boundaries and Crystallization of the SMN Tudor Domain. Acta Cryst. D59: 366-368.
Sprangers, R., Selenko, P., Sattler, M., Sinning, I. & Groves, M.R. (2003)
Glutamate binding affinity of Drosophila metabotropic glutamate receptor is modulated by association with lipid rafts. Proc. Natl. Acad. Sci. USA 100: 10219-10224. Eroglu, C., Brügger, B., Wieland, F. & Sinning, I. (2003)
High-resolution X-Ray and NMR structures of the SMN Tudor Domain: conformational variation in the binding site for symmetrically dimethylated arginines, J. Mol.Biol. 327: 507-520.
Sprangers, R., Groves, M.R., Sinning, I. & Sattler, M. (2003)
Pharmacological characterization and immunoaffinity purification of metabotropic glutamate receptor from Drosophila melanogaster overexpressed in SF9 cells, Prot. Exp. Pur. 30: 275-282.
Panneels, V., Eroglu, C., Cronet, P. & Sinning, I. (2003)
Reconstituted TOM core complex and Tim9/Tim10 complex of mitochondria are sufficient for translocation of the ADP/ATP carrier across membranes, Mol. Biol. Cell 15: 1445-58.
Vasiljev, A., Ahting, U., Nargang, F.E., Go, N.E., Habib, S.J., Kozany, C., Panneels, V., Sinning, I., Prokisch, H., Neupert, W., Nussberger, S. & Rapaport, D. (2003)
Chapter 6: Protein/Protein Interactions, in “Peptide arrays on membrane supports: Synthesis and applications” (J. Koch and M. Mahler, eds.) Springer Verlag Heidelberg, Germany, pp.83-96.
Groves, M., & Sinning, I. (2002)
Distinct modes of Signal Recognition Particle interaction with the Ribosome, Science 297: 1345-8
Pool, M.R., Stumm, J., Fulga, T.A., Sinning, I. & Dobberstein, B. (2002)
Functional reconstitution of purified mGluR overexpressed in the eye of transgenic Drosophila melanogaster, EMBO Rep. 3: 491-496.
Eroglu, C., Cronet, P., Panneels, V., Beaufils, P. & Sinning, I. (2002)
Towards the structure of the mammalian signal recognition particle. Curr. Opin. Struct. Biol.12: 72–81.
Wild, K., Weichenrieder, O., Strub, K., Sinning, I. & Cusack, S. (2002)
Crystal structure of an early protein-RNA assembly complex of human signal recognition particle. Science 294: 598-601.
Wild, K., Sinning, I. & Cusack , S. (2001)
Functional characterization of recombinant chloroplast signal recognition particle. J. Biol. Chem. 276: 27778-86.
Groves M., Mant A., Kuhn A., Koch J, Dubel S., Robinson C. & Sinning I. (2001)
SRbeta coordinates signal sequence release from SRP with ribosome binding to the translocon. EMBO J. 20: 2338-47.
Fulga, T., Sinning, I., Dobberstein, B. & Pool, M.R. (2001)
A spectroscopic method for observing the domain movement of the Rieske iron sulphur protein, Proc. Natl. Acad. Sci. USA 97: 2069-2074.
Brugna, M., Rodgers, S., Schricker, A., Montoya, G., Kazmeier, M., Nitschke, W. & Sinning, I. (2000)
Anionic phospholipids are involved in membrane association of the Signal Recognition Particle receptor FtsY and stimulate its GTPase activity, EMBO J. 19: 531-541.
de Leeuw, E., te Kaat, K., Moser, C., Menestrina, G., Demel, R., de Kruijff, B., Luirink, J. & Sinning, I. (2000)
Deletion of the 6-kDa subunit affects the activity and yield of the bc1 complex from Rhodovulum sulfidophilum. Eur. J. Biochem. 267: 3753-61.
Rodgers, S., Moser, C., Martinez-Julvez, M. & Sinning, I. (2000)
The crystal structure of the conserved GTPase of SRP54 from the archaeon Acidianus ambivalens and its comparison with related structures suggests a model for the SRP/SR receptor complex, Struct. Fold. Des. 8: 515-525.
Montoya, G., te Kaat, K., Moll, R., Schäfer, G. & Sinning, I. (2000)
Crystallization and preliminary X-ray diffraction studies on the conserved GTPase domain of the signal recognition particle from Acidianus ambivalens, Acta Cryst. D55: 1949-1951.
Montoya, G., te Kaat, K., Moll, R., Schäfer, G. & Sinning, I. (1999)
The cytochrome bc1 complex from Rhodovulum sulfidophilum is a dimer with six quinones per monomer and an additional 6-kDa component, Eur. J. Biochem. 259: 709-718.
Montoya, G., te Kaat, K., Rodgers, S., Nitschke, W. & Sinning, I. (1999)
Crystallization and preliminary X-ray diffraction studies of phospho-adenylylsulfate (PAPS) reductase from E. coli. Acta crystallographica. Section D, Biological crystallography, 54(Pt 2), 281–283. https://doi.org/10.1107/s0907444997010019 Montoya, G., Svensson, C., Savage, H., Schwenn, J. D., & Sinning, I. (1998)
Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases. Structure (London, England : 1993), 5(7), 895–906. https://doi.org/10.1016/s0969-2126(97)00244-x Savage, H., Montoya, G., Svensson, C., Schwenn, J. D., & Sinning, I. (1997)
Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases. Structure, 5(7), 895–906. https://doi.org/10.1016/s0969-2126(97)00244-x Savage, H., Montoya, G., Svensson, C., Schwenn, J. D., & Sinning, I. (1997)
Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Nature, 385(6614), 365–368. https://doi.org/10.1038/385365a0 Montoya, G., Svensson, C., Luirink, J., & Sinning, I. (1997)
Expression, crystallization and preliminary X-ray diffraction study of FtsY, the docking protein of the signal recognition particle of E. coli. Proteins, 28(2), 285–288. https://doi.org/10.1002/(sici)1097-0134(199706)28:2<285::aid-prot15>3.0.co;2-e Montoya, G., Svensson, C., Luirink, J., & Sinning, I. (1997)
Membrane association of FtsY, the E. coli SRP receptor. FEBS letters, 416(3), 225–229. https://doi.org/10.1016/s0014-5793(97)01238-6 de Leeuw, E., Poland, D., Mol, O., Sinning, I., ten Hagen-Jongman, C. M., Oudega, B., & Luirink, J. (1997)
The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution, and a comparison with related enzymes. Journal of molecular biology, 272(3), 383–397. https://doi.org/10.1006/jmbi.1997.1243 Kleywegt, G. J., Zou, J. Y., Divne, C., Davies, G. J., Sinning, I., Stâhlberg, J., Reinikainen, T., Srisodsuk, M., Teeri, T. T., & Jones, T. A. (1997)
The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain. Proc Natl Acad Sci USA., 94(21), 11339–11344. https://doi.org/10.1073/pnas.94.21.11339 Moser, C., Mol, O., Goody, R. S., & Sinning, I. (1997)
Two-dimensional structure of light-harvesting complex II (LHII) from the purple bacterium Rhodovulum sulfidophilum and comparison with LHII from Rhodopseudomonas acidophila, Structure 4: 243-252.
Savage, H., Cyrklaff M., Montoya, G., Kühlbrandt, W. & Sinning, I. (1996)
Crystallographic refinement at 2.3 A resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis. Journal of molecular biology, 246(3), 429–457. https://doi.org/10.1006/jmbi.1994.0097 Deisenhofer, J., Epp, O., Sinning, I., & Michel, H. (1995)
Functional significance of arginine 15 in the active site of human class alpha glutathione transferase A1-1. Journal of molecular biology, 247(4), 765–773. https://doi.org/10.1016 Björnestedt, R., Stenberg, G., Widersten, M., Board, P. G., Sinning, I., Jones, T. A., & Mannervik, B. (1995)
Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. Structure, 3(7), 717–727. https://doi.org/10.1016/s0969-2126(01)00206-4 Cameron, A. D., Sinning, I., L'Hermite, G., Olin, B., Board, P. G., Mannervik, B., & Jones, T. A. (1995)
Two-dimensional crystallisation and structure determination of LHII from Rhv. sulfidophilum at 7 Å resolution. in : Photosynthesis : from Light to Biosphere (Mathis, P., ed.) Kluwer Academic Publishers, Dordrecht, Netherlands, pp 239-242.
Savage, H., Cyrklaff, M., Montoya, G., Kuhlbrandt, W. & Sinning, I. (1995)
Two-dimensional crystallization and preliminary structure analysis of light harvesting II (B800-850) complex from the purple bacterium Rhodovulum sulfidophilum. J. Mol. Biol. 250: 1-10.
Montoya, G., Cyrklaff, M. & Sinning, I. (1995)
Crystallization and preliminary X-ray studies on the core proteins of cellobiohydrolase I and endoglucanase I from Trichoderma reesei. J. Mol. Biol. 234: 905-907. Divne, C., Sinning, I., Ståhlberg, J., Pettersson, G., Bailey, M., Siika-aho, M., Margolles-Clark, E., Teeri, T., & Jones, T. A. (1993)
Evidence that serine L223 is involved in the proton transfer pathway to QB in the photosynthetic reaction center of Rhodopseudomonas viridis. Biochemistry, 32(8), 1958–1964. Leibl, W., Sinning, I., Ewald, G., Michel, H., & Breton, J. (1993)
in (Tew, K.D. et al., eds) Structure and function of Glutathione transferases, CRC Press, pp. 29-38. Mannervik, B., Berhane, K., Björnestedt, R., Board, P., Jones, T.A., Kolm, R.H., Olin, B., Sinning, I., Sroga, G.E., Stenberg, G., Tardioli, S. & Widersten, M. (1993)
in (Tew, K.D. et al., eds) Structure and function of Glutathione transferases, CRC Press, pp. 75-86.
Sinning, I., Kleywegt, G.J., Mannervik, B., Board, P. & Jones, T.A. (1993)
Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. J. Mol. Biol. 232: 192-212. Sinning, I., Kleywegt, G.J., Cowan, S.W., Reinemer, P., Dirr, H.W., Huber, R., Gilliland, G.L., Armstrong, R.N., Ji, X., Board, P., Olin, B., Mannervik, B. & Jones, T.A. (1993)
Biochem. Biophys. Acta 1098: 151-158.
Mathis, P., Sinning, I. & Michel, H. (1992)
TIBS 17: 150-54.
Sinning, I. (1992)
Biochem. 30: 9110- 9116.
Baciou, L., Sinning, I. & Sebban, P. (1991)
Biochem. Biophys. Acta 1018: 115-118.
Michel, H., Sinning, I., Koepke, J., Ewald, G. & Fritzsch, G. (1990)
FEBS Lett. 256: 192-194.
Sinning, I., Michel, H., Mathis, P. & Rutherford, A.W. (1990)
in ( M. Michel-Beyerle, ed.) Springer Series in Biophysics: Reaction Center of Photosynthetic Bacteria Vol.6, Springer Verlag, pp. 199-208.
Sinning, I., Koepke, J. & Michel, H. (1990)
in (M. Baltscheffsky, ed.) Current Research in Photosynthesis, Vol.I, Kluwer Acad. Publishers, Netherlands, pp. 173-176.
Sinning, I., Koepke, J., Schiller, B., Mathis, P., Rutherford, A.W. & Michel, H. (1990)
Z. Naturforsch. 45c: 455-458.
Sinning, I., Koepke, J., Schiller, B. & Michel , H. (1990)
Biochem. 28: 5544-5553.
Sinning, I., Michel, H., Mathis, P. & Rutherford, A.W. (1989)
Der Elektronenakzeptorkomplex im photosynthetischen Reaktionszentrum des Purpurbakteriums Rps. viridis , in Wissenschaftl. Forschungsbeiträge Biologie, Biochemie, Chemie, Bd. 32, Verlag Intemann, Prien a. Chiemsee, ISBN 3-926323-36-1.
Sinning, I. (1989)
in (J. Jortner & B. Pullman, eds.) Perspectives in Photosynthesis, Kluwer Academic Publ., Netherlands, pp. 413- 421.
Parak, F., Birk, A., Frolov, E., Goldanskii, V., Sinning, I. & Michel, H. (1989)
J. Biggins (ed.) Progress in Photosynthesis Res. Vol.III, Martinus Nijhoff Publ., Dordrecht,
Sinning, I. & Michel, H. (1987)
Z. Naturforsch. 42c: 751-754.
Sinning, I. & Michel, H. (1987)
Mechanistic insights into RNA surveillance by the canonical poly(A) polymerase Pla1 of the MTREC complex, Nat Commun. 14: 772. doi: doi.org/10.1038/s41467-023-36402-6. Soni, K., Sivadas, A., Horváth, A., Dobrev, N., Hayashi, R., Kiss, L., Simon, B., Wild, K. & Sinning*, I, Fischer*, T. (2023)
Methionine aminopeptidase 2 and its autoproteolysis product have different binding sites on the ribosome, bioRxiv doi:https://doi.org/10.1101/2023.04.06. 535065. Klein, M.A., Wild, K., Kisonaite, M. & Sinning, I. (2023)
Structural inventory of cotranslational protein folding by the eukaryotic RAC complex, Structural inventory of cotranslational protein folding by the eukaryotic RAC complex, Nat. Struct. Mol. Biol. Apr 20. doi: doi.org/10.1038/s41594-023-00973-1 (online ahead of print). Kišonaitė, M., Wild, K., Lapouge, K., Valentín Gesé, G., Kellner, N., Hurt, E. & Sinning, I. (2023)
Trim-Away degrades lysine-less substrates without requiring ligase autoubiquitination, Nat. Commun. 14: 2160. doi: doi.org/10.1038/s41467-023-37504-x. Kiss, L., Rhinesmith, T., Dickson, C.F., Weidenhausen, J., Smyly, S., Luptak, J., Yang, J.C., Maslen, S.L., Sinning, I., Neuhaus, D., Clift, D. & James, L.C. (2023)
Antibacterial peptide CyclomarinA creates toxicity by deregulating the Mycobacterium tuberculosis ClpC1-ClpP1P2 protease. J. Biol. Chem. 298:102202. doi: https://doi.org/10.1016/j.jbc.2022.102202. Taylor, G., Frommherz, Y., Katikaridis, P., Layer, D., Sinning, I., Carroni, M., Weber-Ban, E. & Mogk, A. (2022)
Cryo-EM insights into tail-anchored membrane protein biogenesis in eukaryotes, Curr. Opin. Struct. Biol. 75: 102428. doi: https://doi.org/10.1016/j.sbi.2022.102428. Sinning, I. and McDowell, M.A. (2022)
Extended N-Terminal Acetyltransferase Naa50 in Filamentous Fungi Adds to Naa50 Diversity. Int J Mol Sci. 2022 Sep 16;23(18):10805. doi: doi.org/10.3390/ijms231810805. PMID: 36142717; PMCID: PMC9500918. Weidenhausen J, Kopp J, Ruger-Herreros C, Stein F, Haberkant P, Lapouge K, Sinning I (2022)
High-resolution structures of a thermophilic eukaryotic 80S ribosome reveal atomistic details of translocation, Nat Comms. 13: 476. https://doi.org/10.1038/s41467-022-27967-9.. Kišonaitė, M., Wild, K., Lapouge, K., Ruppert, T. & Sinning, I. (2022)
HYPK promotes the activity of the Nα-acetyltransferase A complex to determine proteostasis of nonAc-X2/N-degron-containing proteins, Sci. Adv. 8:eabn6153. doi: https://doi.org/10.1126/sciadv.abn6153. Miklánková, P., Linster, E., Boyer, J.B., Weidenhausen, J., Mueller, J., Armbruster, L., Lapouge, K., De La Torre, C., Bienvenut, W., Sticht, C., Mann, M., Meinnel, T., Sinning, I., Giglione, C., Hell, R. & Wirtz, M. (2022)
The inner nuclear membrane protein Lem2 coordinates RNA degradation at the nuclear periphery. Nat Struct Mol Biol. 2022 Sep;29(9):910-921. doi: 10.1038/s41594-022-00831-6. Epub 2022 Sep 19. PMID: 36123402; PMCID: PMC9507967. Caballero, L.M., Capella, M., Barrales, R.R., Dobrev, N., van Emden, T., Fischer-Burkart, S., Kinugasa, Y., Hirano, Y., Sinning, I., Fischer, T., Hiraoka, Y. & Braun, S. (2022)
SRP54 mutations induce congenital neutropenia via dominant-negative effects on XBP1 splicing. Blood, 137(10), 1340–1352. https://doi.org/10.1182/blood.2020008115 Schürch, C., Schaefer, T., Müller, J. S., Hanns, P., Arnone, M., Dumlin, A., Schärer, J., Sinning, I., Wild, K., Skokowa, J., Welte, K., Carapito, R., Bahram, S., Konantz, M., & Lengerke, C. (2021)
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Commun Biol 4, 600. https://doi.org/10.1038/s42003-021-02132-y Soni, K., Kempf, G., Manalastas-Cantos, K., Hendricks, A., Flemming, D., Guizetti, J., Simon, B., Frischknecht, F., Svergun, D.I., Wild, K., & Sinning, I. (2021)
Structural and functional characterization of the N-terminal acetyltransferase Naa50. Structure, 29(5), 413–425.e5. https://doi.org/10.1016/j.str.2020.12.004 Weidenhausen, J., Kopp, J., Armbruster, L., Wirtz, M., Lapouge, K., & Sinning, I. (2021)
Structural and functional impact of SRP54 mutations causing severe congenital neutropenia. Structure, 29. doi: http://doi.org/10.1016/j.str.2020.09.008 Juaire, K.D., Lapouge, K., Becker, M.M.M., Kotova, I., Michelhans, M., Carapito, R., Wild, K., Bahram, S. & Sinning, I. (2021)
Structural and molecular mechanisms for membrane protein biogenesis by the Oxa1 superfamily. Nat Struct Mol Biol 28, 234–239. https://doi.org/10.1038/s41594-021-00567-9 McDowell, M.A., Heimes, M. & Sinning, I. (2021)
Structural basis of Naa20 activity towards a canonical NatB substrate. Commun Biol 4, 2. https://doi.org/10.1038/s42003-020-01546-4 Layer, D., Kopp, J., Fontanillo, M., Köhn, M., Lapouge, K. & Sinning, I. (2021)
The zinc-finger protein Red1 orchestrates MTREC submodules and binds the Mtl1 helicase arch domain. Nat Comms. 12: 3456. PMID: 34103492. doi: https://doi.org/10.1038/s41467-021-23565-3 Dobrev, N., Ahmed, Y.L., Sivadas, A., Fischer*, T. & Sinning*, I. (2021)
Cholesterol localization around the metabotropic glutamate receptor 2, J. Phys. Chem. B 24: 9061-9078. PMID: 32954729. Kurth, M., Lolicato, F., Sandoval-Perez, A., Amaya-Espinosa, H., Teslenko, A., Sinning, I., Beck, R., Brügger B. & Aponte-Santamaria, C.A. (2020)
Complexin suppresses spontaneous exocytosis by capturing the membrane-proximal regions of VAMP2 and SNAP25. Cell Reports, 32. https://doi.org/10.1016/j.celrep.2020.107926 Malsam, J., Bärfuss, S., Trimbuch, T.h, Zarebidaki, F., Sonnen, A., Wild, K., Scheutzow, A., Rohland, L., Mayer, M., Sinning, I., Briggs, J., Rosenmund, C. & Söllner, T.H. (2020)
Functional implications of MIR domains in protein O-mannosylation, eLife 9: e61189. PMID: 33357379.
Chiapparino#, A., Grbavac#, A., Jonker, H.R.A., Hackmann, Y., Mortensen, S., Zatorska, E., Schott, A., Stier, G., Saxena, K., Wild, K., Schwalbe, H., Sabine Strahl*, S. & Sinning*, I. (2020)
MetAP-like Ebp1 occupies the human ribosomal tunnel exit and recruits flexible rRNA expansion segments, Nat Comms. 11: 776. PMID: 32034140.
Wild, K., Aleksić, M., Lapouge, K., Juaire, K.D., Flemming, D., Pfeffer, S. & Sinning, I. (2020)
NAA50 is an enzymatically active Nα-acetyltransferase that is crucial for the development and regulation of stress responses, Plant Physiol. 183: 1502-1516.
Armbruster, L., Linster, E., Boyer, J.B., Brünje, A., Eirich, J., Stephan, I., Bienvenut, W.V., Weidenhausen, J., Meinnel, T., Hell, R., Sinning, I., Finkemeier, I., Giglione,G. & Wirtz, M. (2020)
N-terminal acetylation by NatB affects growth and abiotic stress responses in Arabidopsis, Plant Physiol. 182: 792-806. PMID: 31744933.
Huber, M., Bienvenut, W.V., Linster, E., Stephan, I., Armbruster, L., Sticht, C., Layer, D., Lapouge, K., Meinnel, T., Sinning, I., Giglione, C., Hell, R. & Wirtz, M. (2020)
Structural basis for the complex DNA binding behaviour of the plant stem cell regulator WUSCHEL, Nat. Comms. 11: 2223. PMID: 32376862.
Sloan, J., Hakenjos, J.P., Gebert, M., Ermakova, O., Gumiero, A., Stier, G., Wild, K., Sinning*, I. & Lohmann*, J.U. (2020)
Structural basis of tail-anchored membrane protein biogenesis by the GET insertase complex, Mol Cell 80: 72-86.e7. PMID: 32910895.
McDowell*, M.A., Heimes, M., Fiorentino, F., Mehmood, S., Farkas, Á., Coy-Vergara, J., Wu, D., Schmid, V., Heinze, R., Reddy Bolla, J., Wild, K., Flemming, D., Pfeffer, S., Schwappach, B., Robinson, C.V. & Sinning*, I. (2020)
The Arabidopsis Nα-acetyltransferase NAA60 locates to the plasma membrane and is vital for the high salt stress response, New Phytologist, doi: 10.1111/nph.16747. Online ahead of print. PMID: 32548857
Linster#, E., Layer#, D., Bienvenut, W.V., Dinh-Van, T., Weyer, F., Lemhuis, W., Brünje, A., Hoffrichter, M., Miklankova, P., Sindlinger, J., Schwarzer, D., Kopp, J., Lapouge, K., Meinnel, T., Giglione, C., Finkemeier, I., Hell, R., Sinning*, I. & Wirtz*, M. (2020)
The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb, Nat Comms. 11: 1504. PMID: 32198371.
Zhang*, Y., Valentín Gesé*, G., Conz, C., Lapouge, L., Kopp, J., Wölfle, T., Rospert, S. & Sinning, I. (2020)
Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin–ligand-type complexes. Nat Commun 10, 3050. https://doi.org/10.1038/s41467-019-10922-6 Ahmed, Y.L., Thoms, M., Mitterer, V., Sinning, I., & Hurt, E. (2019)
Identification of YvcI as novel RNA pyrophospho-hydrolase from B. subtilis, J. Biol. Chem. 94: 19967-19977. PMID: 31740579.
Frindert, J., Kahloon, M.A., Zhang, Y., Ahmed, Y.L., Sinning, I., & Jäschke, A. (2019)
Novel variants and clinical symptoms in four new ALG3-CDG patients, review of the literature, and identification of AAGRP-ALG3 as a novel ALG3 variant with alanine and glycine-rich N-terminus. Hum Mutat. 40: 938-951. PMID: 31067009.
Himmelreich N, Dimitrov B, Geiger V, Zielonka M, Hutter AM, Beedgen L, Hüllen A, Breuer M, Peters V, Thiemann KC, Hoffmann GF, Sinning I, Dupré T, Vuillaumier-Barrot S, Barrey C, Denecke J, Kölfen W, Düker G, Ganschow R, Lentze MJ, Moore S, Seta N, Ziegler A, Thiel C. (2019)
Reconstitution of the human SRP system and quantitative and systematic analysis of its ribosome interactions, Nucl. Acids Res. 47: 3184-3196.
Wild, K., D. Juaire, K.D., Soni, K., Shanmuganathan, V., Hendriks, A., Segnitz, B., Beckmann, R. & Sinning, I. (2019)
Structure, dynamics, and interactions of large SRP variants (review), Biol. Chem. 401: 63-80. PMID: 31408431.
Wild, K., Becker, MMM, Kempf, G. & Sinning, I. (2019)
DENR-MCTS1 heterodimerization and tRNA recruitment are required for translation reinitiation. PLoS Biol. 16: e2005160. PMID: 29889857.
Ahmed, Y.L., Schleich, S., Bohlen, J., Mandel, N., Simon, B., Sinning*, I. & Teleman*, A.A. (2018)
The Escherichia coli SRP receptor forms a homodimer at the membrane, Structure 26:1440-1450.e5. PMID: 30146170.
Kempf, G., Stjepanovic, G., Hendricks, A., Lapouge, K., & Sinning, I. (2018)
9Å structure of COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments, Elife 6. pii: e26691. Dodonova, S.O., Aderhold, P., Kopp, J., Ganeva, I., Röhling, S., Hagen, W.J.H., Sinning, I., Wieland, F., & Briggs, J.A.G. (2017)
Accumulation of phosphatidylcholine on gut intestinal mucosa surface is not dominated by electrostatic interactions, BBA Biomembranes 1859: 959-965.
Korytowski, A., Abuillan, W., Amadei, F., Makky, A., Gumiero, A., Sinning, I., Gauss, A., Stremmel, W. & Tanaka, M. (2017)
Fe65-PTB2 dimerization mimics Fe65-APP interaction, Front. Mol Neurosci. 10: 140.
Feilen, L.P., Haubrich, K., Strecker, P., Probst, S., Eggert, S., Stier, G., Sinning, I., Konietzko, U., Kins, S., Simon, B. & Wild, K. (2017)
Interaction network of the ribosome assembly machinery from a eukaryotic thermophile. Protein science 26(2), 327–342. https://doi.org/10.1002/pro.3085 Baßler, J., Ahmed, Y.L., Kallas, M., Kornprobst, M., Rodriguez-Calvino, F., Gnädig, M., Thoms, M., Stier, G., Ismail, S., Kharde, S., Castillo, N., Griesel, S., Bastuck, S., Bradatsch, B., Thomson, E., Flemming, D., Sinning, I.* & Hurt, E.* (2017)
Lysine relay mechanism coordinates intermediate transfer in vitamin B6 biosynthesis, Nat. Chem. Biol. 3: 290-294.
Rodrigues, M.J., Windeisen, V., Zhang,Y., Guédez,G., Weber, S., Strohmeier, M., Hanes, J.W., Royant, A., Evans, G., Sinning, I., Ealick, S.E., Begley, T.P. & Tews, I. (2017)
Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome, PlosOne 12: e0183272. Sá-Moura, B., Kornprobst, M., Kharde, S., Ahmed, Y.L., Stier, G., Kunze, R., Sinning*, I. & Hurt*, E. (2017)
Structural basis for 5'-ETS recognition by Utp4 at the early stages of ribosome biogenesis. PLOS ONE 12(6): e0178752. https://doi.org/10.1371/journal.pone.0178752 Calviño, F.R., Kornprobst, M., Schermann, G., Birkle, F., Wild, K., Fischer, T., Hurt, E., Ahmed, Y.L. & Sinning, I. (2017)
Structural basis of HypK regulating N-terminal acetylation by the NatA complex, Nat Comms 8: 15726.
Weyer, F.A., Gumiero, A., Lapouge, K., Bange, G., Kopp, J. & Sinning, I. (2017)
Structural insights into a unique Hsp70/Hsp40 interaction in the eukaryotic ribosome-associated complex, Nat. Struct. Mol. Biol. 24:144-151.
Weyer, F. A., Gumiero, A., Valentín Gesé, G., Lapouge, K. & Sinning, I. (2017)
Structures of human SRP72 reveal its function in co-translational protein targeting, Nucl. Acids Res. 45: 470-481.
Becker, M.M.M., Lapouge, K., Segnitz, B., Wild, K. & Sinning, I. (2017)
Two chaperones locked in an embrace: Structure and function of the ribosome-associated complex RAC, Nat. Struct. Mol. Biol. 24: 611-619.
Zhang, Y., Sinning, I. & Rospert, S. (2017)
Visualizing the assembly pathway of nucleolar pre-60S ribosomes, Cell 171: 1599-1610. Kater, L., Thoms, M., Barrio Garcia, C., Cheng, J., Ismail, S., Ahmed, Y.L., Bange, G., Kressler, D., Berninghausen, O., Sinning, I., Hurt, E. & Beckmann, R. (2017)
Visualizing the earliest steps during nucleolar pre-60S ribosome assembly. Cell 171, 1599–1610. Lukas Kater, Matthias Thoms, Clara Barrio Garcia, Jingdong Cheng, Sherif Ismail, Yasar Luqman Ahmed, Gert Bange, Dieter Kressler, Otto Berninghausen, Irmi Sinning, Ed Hurt and Roland Beckmann (2017)
Concerted removal of the Erb1-Ytm1 complex in ribosome biogenesis relies on an elaborate interface, Nucl. Acids Res. 44: 926-39. Thoms, M., Ahmed. Y.L., Maddi, K., Hurt, E. & Sinning, I. (2016)
Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain, Nat. Comms. 7: 13563. Gumiero, A., Conz, C., Valentín Gesé, G., Zhang, Y., Weyer, F. A., Lapouge, K., Kappes, J., von Plehwe, U., Schermann, G., Fitzke, E., Wölfle, T., Fischer, T., Rospert, S. & Sinning, I. (2016)
RNA-DNA hybrids and RNase H activity are required for efficient DSB repair, Cell 167: 1001-13. Ohle, C., Tesorero, R., Schermann, G., Dobrev, N., Sinning, I. & Fischer, T. (2016)
Structural basis for conserved regulation and adaptation of the signal recognition particle targeting complex, J. Mol. Biol. 428: 2880-97.
Wild, K., Bange, G., Motiejunas, D., Kribelbauer, J., Hendricks, A., Segnitz, B., Wade, R., & Sinning, I. (2016)
A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation, J. Cell Biol. 210: 169-70. Bassler, J., Paternoga, H., Holdermann, I., Thoms, M., Grannemann, S., Barrio-Garcia, C., Nyarko, A., Lee, W. Stier, G., Clark, S., Schraivogel, D., Kallas, M., Beckmann, R., Tollervey, D., Barbar, E., Sinning*, I. & Hurt*, E. (2015)
Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones. Nature communications, 6, 7494. https://doi.org/10.1038/ncomms8494 Pausch, P., Singh, U., Ahmed, Y. L., Pillet, B., Murat, G., Altegoer, F., Stier, G., Thoms, M., Hurt, E., Sinning, I., Bange, G., & Kressler, D. (2015)
Expression of membrane proteins in the eyes of transgenic Drosophila melanogaster. Methods Enzymol. 556: 219-39. Hackmann, Y., Jödicke, L., Panneels, V. & Sinning, I. (2015)
Formation of Disulfide Bridges Drives oligomerization, membrane pore formation and translocation of fibroblast growth factor 2 to cell surfaces, J. Biol. Chem. 290: 8925-37. Müller, H.M., Steringer, J.S., Wegehingel, S., Bleicken, S., Münster, M., Dimou, E., Unger, S., Weidmann, G., Andreas H., Garcia-Saez, A., Wild, K., Sinning, I. & Nickel, W. (2015)
Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocation, Nat Comms. 6: 10133.
Jadhav, B., McKenna, M., Johnson, N., High, S., Sinning, I. & Pool, M.R. (2015)
Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction, Nat Comms. 6: 8875.
Horn, A., Hennig, J., Ahmed, J.L., Stier, G., Wild, K., Sattler, M. & Sinning, I. (2015)
Structure and switch cycle of SRβ as ancestral eukaryotic GTPase associated with secretory membranes, Structure 23: 1838-47.
Jadhav, B., Wild, K., Pool, M.R. & Sinning, I. (2015)
Strukturelle Evolution des Signalerkennungspartikels, Biospektrum 02: 161-163.
Kempf, G., Wild, K. & Sinning, I. (2015)
Symportin 1 chaperones 5S RNP assembly during ribosome biogenesis by occupying an essential rRNA-binding site. Nat Commun 6, 6510. https://doi.org/10.1038/ncomms7510 Calviño, F.R., Kharde, S., Ori, A., Hendricks, A., Wild, K., Kressler, D., Bange, G., Hurt, E., Beck, M. & Sinning, I. (2015)
The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis, Nucl. Acids Res. 43: 7083-95.
Kharde, S., Calviño, F.R., Gumiero, A., Wild, K. & Sinning, I. (2015)
Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions, Nat. Struct. Mol. Biol. 22: 767-73.
Beckert, B., Kedrov, A., Sohmen, D., Kempf, G., Wild, K., Sinning, I., Stahlberg, H., Wilson, D. & Beckmann, R. (2015)
60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein particle, Nat. Commun. 5: 3491. doi: 10.1038/ncomms4491. Leidig, C., Thoms, M., Holdermann, I., Bradatsch, B., Berninghausen, O., Bange, G., Sinning, I., Hurt, E. & Beckmann, R. (2014)
A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation, J. Cell Biol. 207: 481-498. Bassler, J., Paternoga, H., Holdermann, I., Thoms, M., Grannemann, S., Barrio-Garcia, C., Nyarko, A., Stier, G., Clark, S., Schraivogel, D., Kallas, M., Beckmann, R., Tollervey, D., Barbar, E., Sinning*, I. & Hurt*, E. (2014)
An Extended Helical Conformation in Domain 3a of Munc18-1 Provides a Template for SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Complex Assembly. J.Biol.Chem. 289, 9639-9650. https://doi.org/10.1074/jbc.M113.514273 Parisotto, D., Pfau, M., Scheutzow, A., Wild, K., Mayer, M.P., Malsam, J., Sinning, I., & Söllner, T.H. (2014)
Longin and GAF Domains: Structural Evolution and Adaptation to the Subcellular Trafficking Machinery. Traffic 15: 104-21.
De Franceschi, N., Wild, K., Schlacht, A., Dacks, J.B., Sinning, I. & Filippini, F. (2014)
RNA gymnastics in mammalian signal recognition particle assembly, RNA Biol. 11: 1330-1334.
Wild, K. & Sinning, I. (2014)
SRP RNA remodeling by SRP68 explains its role in protein translocation, Science 344: 101-104. DOI:10.1126/science.1249094.
Grotwinkel, J.T., Wild, K., Segnitz, B. & Sinning, I. (2014)
Structure of the tRNA-like bacterial Alu domain Nucl. Acids Res. 42: 12284-94.
Kempf, G., Wild, K. & Sinning, I. (2014)
Consistent mutational paths predict eukaryotic thermostability. BMC evolutionary biology, 13, 7. https://doi.org/10.1186/1471-2148-13-7 van Noort, V., Bradatsch, B., Arumugam, M., Amlacher, S., Bange, G., Creevey, C., Falk, S., Mende, D. R., Sinning, I., Hurt, E., & Bork, P. (2013)
Endoplasmic reticulum Targeting and Insertion of Tail-anchored membrane proteins by the GET pathway. Cold Spring Harb Perspect Biol. 5(8). doi:pii: a013334.
Denic, V., Doetsch, V. & Sinning, I. (2013)
New twist to nuclear import: When two travel together, Com. & Int. Biol. 6:4, e24792; July/August 2013, Landes Bioscience). Bange, G. , Murat, G., Sinning, I., Hurt, E. & Kressler, D. (2013)
SIMIBI Twins in protein targeting and localization, Nat. Struct. Mol. Biol. 20:776-80. doi: 10.1038/nsmb.2605.
Bange, G. & Sinning, I. (2013)
Structural characterization of a eukaryotic co-translational chaperone, the ribosome-associated complex (RAC), Nat. Struct. Mol. Biol. 20:23-8. Leidig, C., Bange, G., Kopp, J., Amlacher, S., Aravind, A., Wickles, S., Witte, G., Hurt, E., Beckmann, R. & Sinning, I. (2013)
Assembly of the eukaryotic PLP-synthase complex from Plasmodium and activation of the Pdx1 enzyme, Structure 20:172-84.
Guédez, G., Hipp, K., Windeisen, V., Derrer, B., Gengenbacher, M., Böttcher, B., Sinning, I., Kappes, B. & Tews, I. (2012)
Chromodomains read the arginine code of post-translational targeting, Nat. Struct. Mol. Biol. 19: 260-3.
Holdermann, I., Meyer, H., Round, A., Wild, K., Sattler, M. & Sinning, I. (2012)
Structure and conservation of the periplasmic targeting factor tic22 protein from plants and cyanobacteria, J. Biol. Chem. 287: 24164-73.
Tripp, J., Hahn, A., Koenig, P., Flinner, N., Bublak, D., Ertel, F., Brouwer, E.M., Mirus, O., Sinning, I., Tews, I. & Schleiff, E. (2012)
Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones, Mol Cell, 2012 Nov 1. doi:pii: S1097-2765(12)00823-4. 10.1016/j.molcel.2012.09.023.
Kityk, R., Kopp, J., Sinning, I. & Mayer, M.P. (2012)
Synchronizing nuclear import of ribosomal proteins with ribosome assembly, Science 338: 666-71. Kressler*, D., Bange, G. Ogawa, Y., Bradatsch, B., Pratte, D., Strauß, D., Amlacher, S., Yoneda,Y., Katahira, J., Sinning, I.*, & Hurt, E.* (2012)
Binding of chloroplast signal recognition particle to a thylakoid membrane protein substrate in aqueous solution and delineation of the cpSRP43-substrate interaction domain. Biochem J. 437(1):149-55.
Cain P, Holdermann I, Sinning I, Johnson AE, Robinson C. (2011)
Drosophila photoreceptor cells exploited for the production of eukaryotic membrane proteins: receptors, transporters and channels. PLoS One. 6(4):e18478.
Panneels V, Kock I, Krijnse-Locker J, Rezgaoui M, Sinning I. (2011)
It takes two to Get3. Structure. 19(10):1353-55. Sinning, I., Bange, G. & Wild, K. (2011)
Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targeting. J Biol Chem. 286(26):23489-97. Epub 2011 May 3.
Stjepanovic G, Kapp K, Bange G, Graf C, Parlitz R, Wild K, Mayer MP, Sinning I. (2011)
Mdm38 is a 14-3-3-Like Receptor and Associates with the Protein Synthesis Machinery at the Inner Mitochondrial Membrane. Traffic. 12 (10):1457-66.
Lupo D, Vollmer C, Deckers M, Mick DU, Tews I, Sinning I, Rehling P. (2011)
Molecular Basis for the Unique Role of the AAA+ Chaperone ClpV in Type VI Protein Secretion. J Biol Chem. 286(34):30010-21.
Pietrosiuk A, Lenherr ED, Falk S, Bönemann G, Kopp J, Zentgraf H, Sinning I, Mogk A. (2011)
Phosphorylation of LRP1 regulates the interaction with Fe65. FEBS Lett. 585:3229-35.
Klug W, Dietl A, Simon B, Sinning I, Wild K. (2011)
Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex. Science. 333(6043):758-62.
Stefer S, Reitz S, Wang F, Wild K, Pang YY, Schwarz D, Bomke J, Hein C, Löhr F, Bernhard F, Denic V, Dötsch V, Sinning I. (2011)
Structural basis for the molecular evolution of SRP-GTPase activation by protein. Nat Struct Mol Biol. 8:1376-80. Bange G, Kümmerer N, Grudnik P, Lindner R, Petzold G, Kressler D, Hurt E, Wild K, Sinning I. (2011)
Substrate binding disrupts dimerization and induces nucleotide exchange of the chloroplast GTPase Toc33. Biochem J. 436(2):313-9.
Oreb M, Höfle A, Koenig P, Sommer MS, Sinning I, Wang F, Tews I, Schnell DJ, Schleiff E. (2011)
Arabidopsis stromal-derived Factor2 (SDF2) is a crucial target of the unfolded protein response in the endoplasmic reticulum. J Biol Chem. 285(23):18113-21.
Schott A, Ravaud S, Keller S, Radzimanowski J, Viotti C, Hillmer S, Sinning I, Strahl S. (2010)
Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of SDF2-like protein from Arabidopsis thaliana. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66(Pt 1):12-4.
Radzimanowski J, Ravaud S, Schott A, Strahl S, Sinning I. (2010)
Conserved properties of polypeptide transport-associated (POTRA) domains derived from cyanobacterial Omp85. J Biol Chem. 285(23):18016-24.
König P, Mirus O, Haarmann R, Sommer MS, Sinning I, Schleiff E, Tews I. (2010)
cpSRP43 is a novel chaperone specific for light-harvesting chlorophyll a,b-binding proteins. J Biol Chem. 285(28):21655-61.
Falk S, Sinning I. (2010)
Defining the structural requirements for ribose 5-phosphate-binding and intersubunit cross-talk of the malarial pyridoxal 5-phosphate synthase. FEBS Lett. 584(19):4169-74.
Derrer B, Windeisen V, Guédez Rodríguez G, Seidler J, Gengenbacher M, Lehmann WD, Rippe K, Sinning I, Tews I, Kappes B. (2010)
FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system. Proc Natl Acad Sci U S A. 107(25):11295-300.
Bange G, Kümmerer N, Engel C, Bozkurt G, Wild K, Sinning I. (2010)
Genetic evidence for functional interaction of the Escherichia coli signal recognition particle receptor with acidic lipids in vivo. J Biol Chem. 285(52):40508-14. Erez E, Stjepanovic G, Zelazny AM, Brügger B, Sinning I, Bibi E. (2010)
Membrane protein expression in the eyes of transgenic flies. Methods Mol Biol. 601:135-47.
Panneels V, Sinning I. (2010)
Signal peptide peptidase (SPP) assembles with substrates and misfolded membrane proteins into distinct oligomeric complexes. Biochem J. 427(3):523-34.
Schrul B, Kapp K, Sinning I, Dobberstein B. (2010)
Structural insights into the assembly of the human and archaeal signal recognition particles. Acta Crystallogr D Biol Crystallogr. 66(Pt 3):295-303.
Wild K, Bange G, Bozkurt G, Segnitz B, Hendricks A, Sinning I. (2010)
The C terminus of Alb3 interacts with the chromodomains 2 and 3 of cpSRP43. J Biol Chem. 285(53):le25-6;
Falk S, Sinning I. (2010)
The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane. J Biol Chem. 285(8):5954-62.
Falk S, Ravaud S, Koch J, Sinning I. (2010)
The structure of Get4 reveals an alpha-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesis. FEBS Lett. 584(8):1509-14. Bozkurt G, Wild K, Amlacher S, Hurt E, Dobberstein B, Sinning I. (2010)
Delivering proteins for export from the cytosol. Nat Rev Mol Cell Biol. 10(4):255-64. Review.
Cross BC, Sinning I, Luirink J, High S. (2009)
Dissection of contributions from invariant amino acids to complex formation and catalysis in the heteromeric pyridoxal 5-phosphate synthase complex from Bacillus subtilis. Biochemistry. 48(9):1928-35.
Wallner S, Neuwirth M, Flicker K, Tews I, Macheroux P. (2009)
Protein targeting by the signal recognition particle. Biol Chem. 390(8):775-82. Review.
Grudnik P, Bange G, Sinning I. (2009)
Signal sequences get active. Nat Chem Biol. 5(3):146-7.
Sinning I, Wild K, Bange G. (2009)
Structural insights into tail-anchored protein binding and membrane insertion by Get3. Proc Natl Acad Sci U S A. 106(50):21131-6. Bozkurt G, Stjepanovic G, Vilardi F, Amlacher S, Wild K, Bange G, Favaloro V, Rippe K, Hurt E, Dobberstein B, Sinning I. (2009)
Targeting of Drosophila rhodopsin requires helix 8 but not the distal C-terminus. PLoS One. 4(7):e6101.
Kock I, Bulgakova NA, Knust E, Sinning I, Panneels V. (2009)
X-ray crystal structure of Saccharomyces cerevisiae Pdx1 provides insights into the oligomeric nature of PLP synthases. FEBS Lett. 583(13):2179-86.
Neuwirth M, Strohmeier M, Windeisen V, Wallner S, Deller S, Rippe K, Sinning I, Macheroux P, Tews I. (2009)
Crystal structure of the human Fe65-PTB1 domain. J Biol Chem. 283(34):23113-20.
Radzimanowski J, Ravaud S, Schlesinger S, Koch J, Beyreuther K, Sinning I, Wild K. (2008)
Membrane curvature induced by Arf1-GTP is essential for vesicle formation. Proc Natl Acad Sci U S A 105, 11731-11736. → Highlighted by the Faculty of 1000 (F1000.com/1119165). http://www.pnas.org/content/105/33/11731 Beck, R, Sun, Z, Adolf, F, Rutz, C, Bassler, J, Wild, K, Sinning, I, Hurt, E, Brügger, B, Béthune, J*, and Wieland, F* (2008)
Mercury-induced crystallization and SAD phasing of the human Fe65-PTB1 domain. Acta Crystallogr Sect F Struct Biol Cryst Commun. 64(Pt 5):382-5.
Radzimanowski J, Ravaud S, Beyreuther K, Sinning I, Wild K. (2008)
On the significance of Toc-GTPase homodimers. J Biol Chem. 283(34):23104-12.
König P, Oreb M, Rippe K, Muhle-Goll C, Sinning I, Schleiff E, Tews I. (2008)
Overproduction, purification, crystallization and preliminary X-ray analysis of human Fe65-PTB2 in complex with the amyloid precursor protein intracellular domain. Acta Crystallogr Sect F Struct Biol Cryst Commun. 64(Pt 5):409-12.
Radzimanowski J, Beyreuther K, Sinning I, Wild K. (2008)
pH Sensitivity of the GTPase Toc33 as a regulatory circuit for protein translocation into chloroplasts. Plant Cell Physiol. 49(12):1917-21.
Bionda T, König P, Oreb M, Tews I, Schleiff E. (2008)
Policing Tic 'n' Toc, the doorway to chloroplasts. Trends Cell Biol. 18(1):19-27. Review.
Oreb M, Tews I, Schleiff E. (2008)
Purification, crystallization and preliminary structural characterization of the periplasmic domain P1 of the Escherichia coli membrane-protein insertase YidC. Acta Crystallogr Sect F Struct Biol Cryst Commun. 64(Pt 2):144-8.
Ravaud S, Wild K, Sinning I. (2008)
Structural basis for a distinct catalytic mechanism in Trypanosoma brucei tryparedoxin peroxidase. J Biol Chem. 283(44):30401-11. Melchers J, Diechtierow M, Fehér K, Sinning I, Tews I, Krauth-Siegel RL, Muhle-Goll C. (2008)
Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43. Science. 321(5886):253-6.
Stengel KF, Holdermann I, Cain P, Robinson C, Wild K, Sinning I. (2008)
Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2. EMBO Rep. 9(11):1134-40.
Radzimanowski J, Simon B, Sattler M, Beyreuther K, Sinning I, Wild K. (2008)
The crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleft. J Biol Chem. 283(14):9350-8.
Ravaud S, Stjepanovic G, Wild K, Sinning I. (2008)
The GTPase cycle of the chloroplast import receptors Toc33/Toc34: implications from monomeric and dimeric structures. Structure. 16(4):585-96.
König P, Oreb M, Höfle A, Kaltofen S, Rippe K, Sinning I, Schleiff E, Tews I. (2008)
Arx1 functions as an unorthodox nuclear export receptor for the 60S pre-ribosomal subunit, Molecular Cell 27:767-79.
Bradatsch B, Katahira J, Kowalinski E, Bange G, Yao W, Sekimoto T, Baumgärtel V, Boese G, Bassler J, Wild K, Peters R, Yoneda Y, Sinning I, Hurt E. (2007)
Canonical Signal Recognition Particle Components Can Be Bypassed for Posttranslational Protein Targeting in Chloroplasts. Plant Cell 19:1635-48.
Tzvetkova-Chevolleau T, Hutin C, Noël LD, Goforth R, Carde JP, Caffarri S, Sinning I, Groves M, Teulon JM, Hoffman NE, Henry R, Havaux M, Nussaume L. (2007)
E. coli SRP-receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix. J. Biol. Chem. 282:32176-184.
Parlitz R, Eitan A, Stjepanovic G, Bahari L, Bange G, Bibi E, Sinning I. (2007)
Expression, purification and preliminary crystallographic characterization of FlhF from Bacillus subtilis, Acta Cryst F. 63: 449-451.
Bange G, Petzold G, Wild K, Sinning I. (2007)
Expression, purification, crystallization and preliminary crystallographic analysis of the proliferation associated protein Ebp1. Acta Cryst F 63: 768-770.
Kowalinski E, Bange G, Wild K, Sinning I. (2007)
Functional analysis of PDX2 from Arabidopsis, a glutaminase involved in vitamin B6 biosynthesis. Plant Physiol. 144:915-25.
Tambasco-Studart M, Tews I, Amrhein N, Fitzpatrick TB. (2007)
Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY. J. Biol. Chem. 282:32168-175.
Bahari L, Parlitz R, Eitan A, Stjepanovic G, Bochkareva ES, Sinning I, Bibi E. (2007)
Protein translocation: Checkpoint role for SRP GTPase activation. Curr. Biol. 17:R980-R982.
Bange G, Wild K, Sinning I. (2007)
Structural and Thermodynamic Insights into the Assembly of the Heteromeric Pyridoxal Phosphate Synthase from Plasmodium falciparum. J Mol Biol. 374:732-48.
Flicker K, Neuwirth M, Strohmeier M, Kappes B, Tews I, Macheroux P. (2007)
The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis. Dev Cell. 12:739-50.
Peplowska K, Markgraf DF, Ostrowicz CW, Bange G, Ungermann C. (2007)
The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions. FEBS Letters 581: 4450-4454.
Kowalinski E, Bange G, Bradatsch B, Hurt E, Wild K, Sinning I. (2007)
The crystal structure of the third SRP GTPase FlhF reveals a homodimer with bound GTP. Proc. Natl. Acad.Sci. USA 104: 13621-13625.
Bange G, Petzold G, Wild K, Parlitz RO, Sinning I. (2007)
The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site. FEBS Letters 581:5671-6.
Stengel KF, Holdermann I, Wild K, Sinning I. (2007)
The structure of the regulatory domain of the adenylyl cyclase Rv1264 from Mycobacterium tuberculosis with bound oleic acid. J. Mol. Biol. 369:1282-95.
Findeisen F, Linder JU, Schultz A, Schultz JE, Brügger B, Wieland F, Sinning I, Tews I. (2007)
Thermodynamic characterization of the protein-protein interaction in the heteromeric Bacillus subtilis pyridoxalphosphate synthase. Biochemistry 46:5131-9.
Neuwirth M, Flicker K, Strohmeier M, Tews I, Macheroux P. (2007)
Two independent routes of de novo vitamin B6 biosynthesis: not that different after all. Biochem J. 407:1-13.
Fitzpatrick TB, Amrhein N, Kappes B, Macheroux P, Tews I, Raschle T. (2007)
Fatty acid regulation of adenylyl cyclase Rv2212 from Mycobacterium tuberculosis H37Rv. FEBS J. 273(18):4219-28.
Motaal A, Tews I, Schultz JE, Linder JU. (2006)
Following the signal sequence from ribosomal tunnel exit to signal recognition particle. Nature. 444(7118):507-11.
Halic M, Blau M, Becker T, Mielke T, Pool MR, Wild K, Sinning I, Beckmann R. (2006)
Signal recognition particle receptor exposes the ribosomal translocon binding site. Science. 312(5774):745-7.
Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, Sinning I, Beckmann R. (2006)
Structure of a bacterial pyridoxal 5'-phosphate synthase complex. Proc Natl Acad Sci U S A. 103(51):19284-9.
Strohmeier M, Raschle T, Mazurkiewicz J, Rippe K, Sinning I, Fitzpatrick TB, Tews I. (2006)
The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64. EMBO J. 25(9):1836-47.
Qbadou S, Becker T, Mirus O, Tews I, Soll J, Schleiff E. (2006)
The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains. J Biol Chem. 281(13):8898-906.
Schlenker O, Hendricks A, Sinning I, Wild K. (2006)
Vitamin B6 biosynthesis by the malaria parasite Plasmodium falciparum: Biochemical and structural insights. J Biol Chem. 281(6):3633-41.
Gengenbacher M, Fitzpatrick TB, Raschle T, Flicker K, Sinning I, Müller S, Macheroux P, Tews I, Kappes B. (2006)
The structure of a pH sensing mycobacterial adenylyl cyclase holoenzyme, Science 308: 1020-1023.
Tews, I., Findeisen, F., Sinning, I., Schultz A., Schultz, J.E. & Linder, J.U. (2005)
A structural step into the SRP cycle, Mol. Microbiol. 53: 357-63.
Wild, K., Rosendal, K. & Sinning, I. (2004)
Co-translational protein targeting: SRP meets the ribosome, Nat. Struct. Mol. Biol. 11: 1049-53.
Wild, K., Halic, M., Sinning, I. & Beckmann, R. (2004)
Crystallization and preliminary X-ray diffraction studies of the crenarchaeal SRP core, Acta Cryst. D60: 140-143.
Rosendal, K.R., Sinning, I. & Wild, K. (2004)
Crystallization of a Golgi-associated PR-1 related protein (GAPR-1) that localizes to lipid-enriched microdomains, Acta Cryst. D60: 730–732.
Groves, M.R., Kuhn, A., Hendricks, A., Radke, S., Serrano, R.L., Helms, J.B & Sinning, I. (2004)
Signal recognition particle mediates posttranslational targeting in eukaryotes, EMBO J. 23:2755-64.
Abell. B., Pool., M., Schlenker, O., Sinning, I. & High, S. (2004)
SRP-mediated protein targeting: structure and function revisited, BBA Mol. Cell Res. 1694: 17-35.
Luirink, J. & Sinning, I. (2004)
Structural analysis of the human Golgi-associated plant pathogenesis related protein GAPR-1 implicates dimerization as a regulatory mechanism, J. Mol. Biol. 339: 173-83.
Serrano, R.L., Kuhn, A., Hendricks, A., Helms, J.B., Sinning, I. & Groves, M.R. (2004)
Structural biology. Surprising news from the PCC. Science 303: 320-2.
Dobberstein, B. & Sinning. I. (2004)
Choline head groups stabilize the matrix loop regions of the ATP/ADP carrier ScAAC2. Biochem. Biophys. Res. Com. 300: 65-74.
Panneels, V., Schüssler, U., Costagliola, S. & Sinning, I. (2003)
Crystal structure of the complete core of archaeal signal recognition particle and implications for inter-domain communication, Proc. Natl. Acad. Sci. USA 100: 14701-14706.
Rosendal, K.R., Wild, K., Montoya, G. & Sinning, I. (2003)
Definition of Domain Boundaries and Crystallization of the SMN Tudor Domain. Acta Cryst. D59: 366-368.
Sprangers, R., Selenko, P., Sattler, M., Sinning, I. & Groves, M.R. (2003)
Glutamate binding affinity of Drosophila metabotropic glutamate receptor is modulated by association with lipid rafts. Proc. Natl. Acad. Sci. USA 100: 10219-10224. Eroglu, C., Brügger, B., Wieland, F. & Sinning, I. (2003)
High-resolution X-Ray and NMR structures of the SMN Tudor Domain: conformational variation in the binding site for symmetrically dimethylated arginines, J. Mol.Biol. 327: 507-520.
Sprangers, R., Groves, M.R., Sinning, I. & Sattler, M. (2003)
Pharmacological characterization and immunoaffinity purification of metabotropic glutamate receptor from Drosophila melanogaster overexpressed in SF9 cells, Prot. Exp. Pur. 30: 275-282.
Panneels, V., Eroglu, C., Cronet, P. & Sinning, I. (2003)
Reconstituted TOM core complex and Tim9/Tim10 complex of mitochondria are sufficient for translocation of the ADP/ATP carrier across membranes, Mol. Biol. Cell 15: 1445-58.
Vasiljev, A., Ahting, U., Nargang, F.E., Go, N.E., Habib, S.J., Kozany, C., Panneels, V., Sinning, I., Prokisch, H., Neupert, W., Nussberger, S. & Rapaport, D. (2003)
Chapter 6: Protein/Protein Interactions, in “Peptide arrays on membrane supports: Synthesis and applications” (J. Koch and M. Mahler, eds.) Springer Verlag Heidelberg, Germany, pp.83-96.
Groves, M., & Sinning, I. (2002)
Distinct modes of Signal Recognition Particle interaction with the Ribosome, Science 297: 1345-8
Pool, M.R., Stumm, J., Fulga, T.A., Sinning, I. & Dobberstein, B. (2002)
Functional reconstitution of purified mGluR overexpressed in the eye of transgenic Drosophila melanogaster, EMBO Rep. 3: 491-496.
Eroglu, C., Cronet, P., Panneels, V., Beaufils, P. & Sinning, I. (2002)
Towards the structure of the mammalian signal recognition particle. Curr. Opin. Struct. Biol.12: 72–81.
Wild, K., Weichenrieder, O., Strub, K., Sinning, I. & Cusack, S. (2002)
Crystal structure of an early protein-RNA assembly complex of human signal recognition particle. Science 294: 598-601.
Wild, K., Sinning, I. & Cusack , S. (2001)
Functional characterization of recombinant chloroplast signal recognition particle. J. Biol. Chem. 276: 27778-86.
Groves M., Mant A., Kuhn A., Koch J, Dubel S., Robinson C. & Sinning I. (2001)
SRbeta coordinates signal sequence release from SRP with ribosome binding to the translocon. EMBO J. 20: 2338-47.
Fulga, T., Sinning, I., Dobberstein, B. & Pool, M.R. (2001)
A spectroscopic method for observing the domain movement of the Rieske iron sulphur protein, Proc. Natl. Acad. Sci. USA 97: 2069-2074.
Brugna, M., Rodgers, S., Schricker, A., Montoya, G., Kazmeier, M., Nitschke, W. & Sinning, I. (2000)
Anionic phospholipids are involved in membrane association of the Signal Recognition Particle receptor FtsY and stimulate its GTPase activity, EMBO J. 19: 531-541.
de Leeuw, E., te Kaat, K., Moser, C., Menestrina, G., Demel, R., de Kruijff, B., Luirink, J. & Sinning, I. (2000)
Deletion of the 6-kDa subunit affects the activity and yield of the bc1 complex from Rhodovulum sulfidophilum. Eur. J. Biochem. 267: 3753-61.
Rodgers, S., Moser, C., Martinez-Julvez, M. & Sinning, I. (2000)
The crystal structure of the conserved GTPase of SRP54 from the archaeon Acidianus ambivalens and its comparison with related structures suggests a model for the SRP/SR receptor complex, Struct. Fold. Des. 8: 515-525.
Montoya, G., te Kaat, K., Moll, R., Schäfer, G. & Sinning, I. (2000)
Crystallization and preliminary X-ray diffraction studies on the conserved GTPase domain of the signal recognition particle from Acidianus ambivalens, Acta Cryst. D55: 1949-1951.
Montoya, G., te Kaat, K., Moll, R., Schäfer, G. & Sinning, I. (1999)
The cytochrome bc1 complex from Rhodovulum sulfidophilum is a dimer with six quinones per monomer and an additional 6-kDa component, Eur. J. Biochem. 259: 709-718.
Montoya, G., te Kaat, K., Rodgers, S., Nitschke, W. & Sinning, I. (1999)
Crystallization and preliminary X-ray diffraction studies of phospho-adenylylsulfate (PAPS) reductase from E. coli. Acta crystallographica. Section D, Biological crystallography, 54(Pt 2), 281–283. https://doi.org/10.1107/s0907444997010019 Montoya, G., Svensson, C., Savage, H., Schwenn, J. D., & Sinning, I. (1998)
Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases. Structure (London, England : 1993), 5(7), 895–906. https://doi.org/10.1016/s0969-2126(97)00244-x Savage, H., Montoya, G., Svensson, C., Schwenn, J. D., & Sinning, I. (1997)
Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases. Structure, 5(7), 895–906. https://doi.org/10.1016/s0969-2126(97)00244-x Savage, H., Montoya, G., Svensson, C., Schwenn, J. D., & Sinning, I. (1997)
Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Nature, 385(6614), 365–368. https://doi.org/10.1038/385365a0 Montoya, G., Svensson, C., Luirink, J., & Sinning, I. (1997)
Expression, crystallization and preliminary X-ray diffraction study of FtsY, the docking protein of the signal recognition particle of E. coli. Proteins, 28(2), 285–288. https://doi.org/10.1002/(sici)1097-0134(199706)28:2<285::aid-prot15>3.0.co;2-e Montoya, G., Svensson, C., Luirink, J., & Sinning, I. (1997)
Membrane association of FtsY, the E. coli SRP receptor. FEBS letters, 416(3), 225–229. https://doi.org/10.1016/s0014-5793(97)01238-6 de Leeuw, E., Poland, D., Mol, O., Sinning, I., ten Hagen-Jongman, C. M., Oudega, B., & Luirink, J. (1997)
The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution, and a comparison with related enzymes. Journal of molecular biology, 272(3), 383–397. https://doi.org/10.1006/jmbi.1997.1243 Kleywegt, G. J., Zou, J. Y., Divne, C., Davies, G. J., Sinning, I., Stâhlberg, J., Reinikainen, T., Srisodsuk, M., Teeri, T. T., & Jones, T. A. (1997)
The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain. Proc Natl Acad Sci USA., 94(21), 11339–11344. https://doi.org/10.1073/pnas.94.21.11339 Moser, C., Mol, O., Goody, R. S., & Sinning, I. (1997)
Two-dimensional structure of light-harvesting complex II (LHII) from the purple bacterium Rhodovulum sulfidophilum and comparison with LHII from Rhodopseudomonas acidophila, Structure 4: 243-252.
Savage, H., Cyrklaff M., Montoya, G., Kühlbrandt, W. & Sinning, I. (1996)
Crystallographic refinement at 2.3 A resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis. Journal of molecular biology, 246(3), 429–457. https://doi.org/10.1006/jmbi.1994.0097 Deisenhofer, J., Epp, O., Sinning, I., & Michel, H. (1995)
Functional significance of arginine 15 in the active site of human class alpha glutathione transferase A1-1. Journal of molecular biology, 247(4), 765–773. https://doi.org/10.1016 Björnestedt, R., Stenberg, G., Widersten, M., Board, P. G., Sinning, I., Jones, T. A., & Mannervik, B. (1995)
Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. Structure, 3(7), 717–727. https://doi.org/10.1016/s0969-2126(01)00206-4 Cameron, A. D., Sinning, I., L'Hermite, G., Olin, B., Board, P. G., Mannervik, B., & Jones, T. A. (1995)
Two-dimensional crystallisation and structure determination of LHII from Rhv. sulfidophilum at 7 Å resolution. in : Photosynthesis : from Light to Biosphere (Mathis, P., ed.) Kluwer Academic Publishers, Dordrecht, Netherlands, pp 239-242.
Savage, H., Cyrklaff, M., Montoya, G., Kuhlbrandt, W. & Sinning, I. (1995)
Two-dimensional crystallization and preliminary structure analysis of light harvesting II (B800-850) complex from the purple bacterium Rhodovulum sulfidophilum. J. Mol. Biol. 250: 1-10.
Montoya, G., Cyrklaff, M. & Sinning, I. (1995)
Crystallization and preliminary X-ray studies on the core proteins of cellobiohydrolase I and endoglucanase I from Trichoderma reesei. J. Mol. Biol. 234: 905-907. Divne, C., Sinning, I., Ståhlberg, J., Pettersson, G., Bailey, M., Siika-aho, M., Margolles-Clark, E., Teeri, T., & Jones, T. A. (1993)
Evidence that serine L223 is involved in the proton transfer pathway to QB in the photosynthetic reaction center of Rhodopseudomonas viridis. Biochemistry, 32(8), 1958–1964. Leibl, W., Sinning, I., Ewald, G., Michel, H., & Breton, J. (1993)
in (Tew, K.D. et al., eds) Structure and function of Glutathione transferases, CRC Press, pp. 29-38. Mannervik, B., Berhane, K., Björnestedt, R., Board, P., Jones, T.A., Kolm, R.H., Olin, B., Sinning, I., Sroga, G.E., Stenberg, G., Tardioli, S. & Widersten, M. (1993)
in (Tew, K.D. et al., eds) Structure and function of Glutathione transferases, CRC Press, pp. 75-86.
Sinning, I., Kleywegt, G.J., Mannervik, B., Board, P. & Jones, T.A. (1993)
Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. J. Mol. Biol. 232: 192-212. Sinning, I., Kleywegt, G.J., Cowan, S.W., Reinemer, P., Dirr, H.W., Huber, R., Gilliland, G.L., Armstrong, R.N., Ji, X., Board, P., Olin, B., Mannervik, B. & Jones, T.A. (1993)
Biochem. Biophys. Acta 1098: 151-158.
Mathis, P., Sinning, I. & Michel, H. (1992)
TIBS 17: 150-54.
Sinning, I. (1992)
Biochem. 30: 9110- 9116.
Baciou, L., Sinning, I. & Sebban, P. (1991)
Biochem. Biophys. Acta 1018: 115-118.
Michel, H., Sinning, I., Koepke, J., Ewald, G. & Fritzsch, G. (1990)
FEBS Lett. 256: 192-194.
Sinning, I., Michel, H., Mathis, P. & Rutherford, A.W. (1990)
in ( M. Michel-Beyerle, ed.) Springer Series in Biophysics: Reaction Center of Photosynthetic Bacteria Vol.6, Springer Verlag, pp. 199-208.
Sinning, I., Koepke, J. & Michel, H. (1990)
in (M. Baltscheffsky, ed.) Current Research in Photosynthesis, Vol.I, Kluwer Acad. Publishers, Netherlands, pp. 173-176.
Sinning, I., Koepke, J., Schiller, B., Mathis, P., Rutherford, A.W. & Michel, H. (1990)
Z. Naturforsch. 45c: 455-458.
Sinning, I., Koepke, J., Schiller, B. & Michel , H. (1990)
Biochem. 28: 5544-5553.
Sinning, I., Michel, H., Mathis, P. & Rutherford, A.W. (1989)
Der Elektronenakzeptorkomplex im photosynthetischen Reaktionszentrum des Purpurbakteriums Rps. viridis , in Wissenschaftl. Forschungsbeiträge Biologie, Biochemie, Chemie, Bd. 32, Verlag Intemann, Prien a. Chiemsee, ISBN 3-926323-36-1.
Sinning, I. (1989)
in (J. Jortner & B. Pullman, eds.) Perspectives in Photosynthesis, Kluwer Academic Publ., Netherlands, pp. 413- 421.
Parak, F., Birk, A., Frolov, E., Goldanskii, V., Sinning, I. & Michel, H. (1989)
J. Biggins (ed.) Progress in Photosynthesis Res. Vol.III, Martinus Nijhoff Publ., Dordrecht,
Sinning, I. & Michel, H. (1987)
Z. Naturforsch. 42c: 751-754.
Sinning, I. & Michel, H. (1987)
Collaborations
- Seiamak Bahram, Univ. Strasbourg, France
- Michael Boutros, DKFZ Heidelberg
- Britta Brügger, BZH
- Raphael Carapito, Univ. Strasbourg, France
- Iris Finkemeier, Univ. Münster
- Tamas Fischer, Univ. Canberra, Australia
- Mark Helm, Univ. Mainz
- Andres Jäschke, IPMB Univ. Heidelberg
- Christof Niehrs, DKFZ Heidelberg
- Carol Robinson, Univ. Oxford, UK
- Sabine Rospert, Univ. Freiburg
- Harald Schwalbe, Univ. Frankfurt
- Blanche Schwappach, Univ. Göttingen
- Sabine Strahl, COS Univ. Heidelberg
- Henning Urlaub, MPI BPC and Univ. Göttingen
- Markus Wirtz, COS Univ. Heidelberg
Funding
Current:
- Leibniz Programme of the DFG
- SFB 1324
- TRR 319
- FOR 2509
- (recently finished: SFB 1036, TRR 83)
Open Positions
Please use the Application Form (PDF) provided and fill and save it with Acrobat Reader.
Contact
Biochemie-Zentrum
der Universität Heidelberg (BZH)
Im Neuenheimer Feld 328
69120 Heidelberg
der Universität Heidelberg (BZH)
Im Neuenheimer Feld 328
69120 Heidelberg
Office:
+49 6221 54-4781 Fax:
+49 6221 54-4790 E-Mail:
irmi.sinning@bzh.uni-heidelberg.deSekretariat: Anja Weber
Office:
+49 6221 54-4780 Fax:
+49 6221 54-4790 E-Mail:
anja.weber@bzh.uni-heidelberg.de