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Groupleader: Mandy Jeske
Mandy Jeske
piRNA biogenesis and function
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Research
1. Research group April 2022
2. Protein crystal
3. Electron density map
4. Drosophila egg chambers with Vasa staining
5. Scholar Goggler by Ryan Morin
6. AF3 model of an RNA helicase complex
In the lab, we are using a multidisciplinary approach to investigate proteins and protein complexes with essential functions during germ cell formation and early embryonic development of Drosophila. The main research focusses on understanding molecular mechanism underlying piRNA biogenesis and piRNA-mediated silencing of transposon mRNAs, processes which are highly critical during gametogenesis and early animal development.
In particular, we are currently focusing our studies on LOTUS domain-containing proteins (Kubíková et al., 2020) and on ATP-dependent RNA helicases. To unravel the molecular mechanisms of how these proteins function in the piRNA pathway, we combine RNA/protein biochemistry, enzymology, X-ray crystallography, structural modeling using AlphaFold-multimer, and cell culture techniques with Drosophila genetics.
@Jeske_Lab @mandyjeske.bsky.social
CV
| 1998 - 2005 | Biochemistry Studies at University Halle-Wittenberg |
| 2005 - 2010 | PhD at the University Halle-Wittenberg with Elmar Wahle |
| 2010 - 2017 |
Postdoc at the EMBL with Anne Ephrussi and Christoph W. Müller (EIPOD Developmental/Structural biology) |
| since Dec 2017 | Emmy Noether Group Leader at the Heidelberg University Biochemistry Center (BZH) |
Lab Members
Asen Garbelyanski
PhD student
PhD student
Lab:Room 422
/ Phone: +49 6221 54-4739
Mail:asen.garbelyanski@bzh.uni-heidelberg.de
Sherif Ismail
postdoc
postdoc
Lab:Room 424
/ Phone: +49 6221 54-6763
Mail:sherif.ismail@bzh.uni-heidelberg.de
Publications
Molecular insights into the Drosophila piRNA pathway via systematic ReLo protein interaction screening and structure prediction.
Nucleic Acids Research, 53 (19), gkaf993
Salgania, H.K., Metz, J., Lingren, E., Bleischwitz, C., Hauser, D., Oliveras Máté, K., Bollack, D., Lahr, F., Bruckmann, A., Garbelyanski, A., Jeske, M. (2025)
Recurrent innovation of protein-protein interactions in the Drosophila piRNA pathway.
EMBO J, 10.1038/S44318-025-00439-8.
Riedelbauch S, Masser S, Fasching S, Lin SY, Salgania HK, Aarup M, Ebert A, Jeske M, Levine MT, Stelzl U, Andersen P. (2025)
Probing direct interactions between nuclear proteins in cells with nxReLo.
Proceedings of the National Academy of Sciences 122 (48): e2518711122.
Ismail, S., Kubíková, J., Maichel, M., Andersen, P., Jeske, M. (2025)
ReLo: Analyse direkter Protein-Protein-Interaktionen durch Relokalisation.
BIOspektrum. 30, 769–771
Miederer, L., and Jeske, M. (2024)
ReLo is a simple and rapid colocalization assay to identify and characterize direct protein–protein interactions.
Nature Communications. 15(1):2875
Salgania, H.K., Metz, J., Jeske, M. (2024)
RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system.
Nucleic Acids Research, 51 (8), 3950–3970.
Pekovic, F., Rammelt, C., Kubíková, J., Metz, J., Jeske, M., Wahle, E. (2023)
Structural basis for binding of Drosophila Smaug to the GPCR Smoothened and to the germline inducer Oskar.
Proceedings of the National Academy of Sciences 120: e2304385120.
Kubíková, J., Ubartaitė, G., Metz, J., Jeske, M. (2023)
Molekulare Funktionen von Keimbahn-spezifischen Proteinen.
BIOspektrum. 27, 101.
Jeske, M. (2021)
LOTUS-domain proteins - Developmental effectors from a molecular perspective.
Biol. Chem. 402, 7–23.
Kubíková, J., Reinig, R., Salgania, H.K., and Jeske, M. (2020)
The LOTUS domain is a conserved DEAD-box RNA helicase regulator essential for the recruitment of Vasa to the germ plasm and nuage.
Genes Dev. 31(9), 939-952.
Jeske, M., Müller, C.W., Ephrussi, A. (2017)
The crystal structure of the Drosophila germline-inducer Oskar identifies two domains with distinct Vasa helicase- and RNA-binding activities.
Cell Reports, 12(4), 587-98.
Jeske, M., Bordi, M., Glatt, S., Müller, S., Rybin, V., Müller, C.W., Ephrussi, A. (2015)
Assaying mRNA deadenylation in vitro.
Methods Mol. Biol. 1125, 297–311.
Jeske, M., Temme, C., Wahle, E. (2014)
Identification of Drosophila and human 7-methyl GMP-specific nucleotidases.
J. Biol. Chem. 288(4), 2441-2451.
Buschmann, J., Moritz, B., Jeske, M., Lilie, H., Schierhorn, A., Wahle, E. (2013)
Smaug assembles an ATP-dependent stable complex repressing nanos mRNA translation at multiple levels.
EMBO J. 30(1), 90-103.
Jeske, M., Moritz, B., Anders, A., Wahle, E. (2011)
Cell-free deadenylation assays with Drosophila embryo extracts.
Meth. Enzymol. 448, 107-118.
Jeske, M., Wahle, E. (2008)
Rapid ATP-dependent deadenylation of nanos mRNA in a cell-free system from Drosophila embryos.
J. Biol. Chem. 281(35), 25124-25133.
Jeske, M., Meyer, S., Temme, C., Freudenreich, D., Wahle, E. (2006)
Nucleic Acids Research, 53 (19), gkaf993
Salgania, H.K., Metz, J., Lingren, E., Bleischwitz, C., Hauser, D., Oliveras Máté, K., Bollack, D., Lahr, F., Bruckmann, A., Garbelyanski, A., Jeske, M. (2025)
Recurrent innovation of protein-protein interactions in the Drosophila piRNA pathway.
EMBO J, 10.1038/S44318-025-00439-8.
Riedelbauch S, Masser S, Fasching S, Lin SY, Salgania HK, Aarup M, Ebert A, Jeske M, Levine MT, Stelzl U, Andersen P. (2025)
Probing direct interactions between nuclear proteins in cells with nxReLo.
Proceedings of the National Academy of Sciences 122 (48): e2518711122.
Ismail, S., Kubíková, J., Maichel, M., Andersen, P., Jeske, M. (2025)
ReLo: Analyse direkter Protein-Protein-Interaktionen durch Relokalisation.
BIOspektrum. 30, 769–771
Miederer, L., and Jeske, M. (2024)
ReLo is a simple and rapid colocalization assay to identify and characterize direct protein–protein interactions.
Nature Communications. 15(1):2875
Salgania, H.K., Metz, J., Jeske, M. (2024)
RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system.
Nucleic Acids Research, 51 (8), 3950–3970.
Pekovic, F., Rammelt, C., Kubíková, J., Metz, J., Jeske, M., Wahle, E. (2023)
Structural basis for binding of Drosophila Smaug to the GPCR Smoothened and to the germline inducer Oskar.
Proceedings of the National Academy of Sciences 120: e2304385120.
Kubíková, J., Ubartaitė, G., Metz, J., Jeske, M. (2023)
Molekulare Funktionen von Keimbahn-spezifischen Proteinen.
BIOspektrum. 27, 101.
Jeske, M. (2021)
LOTUS-domain proteins - Developmental effectors from a molecular perspective.
Biol. Chem. 402, 7–23.
Kubíková, J., Reinig, R., Salgania, H.K., and Jeske, M. (2020)
The LOTUS domain is a conserved DEAD-box RNA helicase regulator essential for the recruitment of Vasa to the germ plasm and nuage.
Genes Dev. 31(9), 939-952.
Jeske, M., Müller, C.W., Ephrussi, A. (2017)
The crystal structure of the Drosophila germline-inducer Oskar identifies two domains with distinct Vasa helicase- and RNA-binding activities.
Cell Reports, 12(4), 587-98.
Jeske, M., Bordi, M., Glatt, S., Müller, S., Rybin, V., Müller, C.W., Ephrussi, A. (2015)
Assaying mRNA deadenylation in vitro.
Methods Mol. Biol. 1125, 297–311.
Jeske, M., Temme, C., Wahle, E. (2014)
Identification of Drosophila and human 7-methyl GMP-specific nucleotidases.
J. Biol. Chem. 288(4), 2441-2451.
Buschmann, J., Moritz, B., Jeske, M., Lilie, H., Schierhorn, A., Wahle, E. (2013)
Smaug assembles an ATP-dependent stable complex repressing nanos mRNA translation at multiple levels.
EMBO J. 30(1), 90-103.
Jeske, M., Moritz, B., Anders, A., Wahle, E. (2011)
Cell-free deadenylation assays with Drosophila embryo extracts.
Meth. Enzymol. 448, 107-118.
Jeske, M., Wahle, E. (2008)
Rapid ATP-dependent deadenylation of nanos mRNA in a cell-free system from Drosophila embryos.
J. Biol. Chem. 281(35), 25124-25133.
Jeske, M., Meyer, S., Temme, C., Freudenreich, D., Wahle, E. (2006)
Funding
Our research is funded by the DFG, the Chica and Heinz Schaller Foundation, and the Health+Life Science Alliance Heidelberg Mannheim.
1. DFG
2. CHS
3. Health + Life Science Alliance
Open Positions
Interested Trainees and highly motivated Bachelor and Master students are welcome to join our lab. Please contact me by mail: jeske@bzh.uni-heidelberg.de
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 54-4728 Fax:
+49 6221 54-4369 E-Mail:
jeske@bzh.uni-heidelberg.de