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Groupleader: Johannes Lechner

Kinetochore and Chromosome Segregation / ESI MS Service 

Group Leader Johannes Lechner

Johannes Lechner

Kinetochore and Chromosome Segregation / ESI MS Service

  • Research
  • CV
  • Lab Members
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Research 


The kinetochore is a specialized chromosomal structure that facilitates chromosome attachment and movement along spindle microtubules during chromosome segregation. Furthermore, the kinetochore communicates the actual state of its interaction with the spindle to a cell cycle regulating machinery. It is the first member of a signaling cascade that inhibits sister chromatid separation (the beginning of anaphase) if chromosomes lack a stable bi-polar spindle attachment. A defect in this checkpoint function has been correlated to human cancers.
My group analyses the protein composition and structure of the S. cerevisiae kinetochore by mass spectroscopy and the function of individual kinetochore proteins applying cell and molecular biological methods. 

Download BZH Report Lechner 2014-2016

 

CV 


Academic Training and Positions

1975-1981 Study of Chemistry at the University of Regensburg
1981-1985 PhD Student at the University of Regensburg (Prof. Dr. M. Sumper)
1985-1987 Post-Doc. University of Regensburg (Prof. Dr. M. Sumper)
1987-1990 Post-Doc. University of California, Santa Barbara (Prof. Dr. J. Carbon)
1991-1994 Research assistent at the University of Regensburg
1994 Habilitation in Biochemistry 
1994-1999 Senior research assistent at the University of Regensburg
since 1999 Group leader at the Heidelberg University Biochemistry Center (BZH)

Lab Members 



Petra Ihrig
TA

Lab:Room 121 / Phone: +49 6221 54-4156
Office:Room 101 / Phone: +49 6221 54-4325
Mail:petra.ihrig@bzh.uni-heidelberg.de

 RoomPhone
LAB 121 +49 6221 54-4156
OFFICE 101 +49 6221 54-4325
E-Mail petra.ihrig@bzh.uni-heidelberg.de
Britta Klem
TA

Lab:Room 122 / Phone: +49 6221 54-4336
Mail:britta.klem@bzh.uni-heidelberg.de

 RoomPhone
LAB 122 +49 6221 54-4336
E-Mail britta.klem@bzh.uni-heidelberg.de
Sarina Norell
PhD student

Lab:Room 122 / Phone: +49 6221 54-4336
Office:Room 103 / Phone: +49 6221 54-4164
Mail:sarina.norell@bzh.uni-heidelberg.de

 RoomPhone
LAB 122 +49 6221 54-4336
OFFICE 103 +49 6221 54-4164
E-Mail sarina.norell@bzh.uni-heidelberg.de
Jennifer Ortiz
postdoc

Lab:Room 122 / Phone: +49 6221 54-5424
Mail:jennifer.ortiz@bzh.uni-heidelberg.de

 RoomPhone
LAB 122 +49 6221 54-5424
E-Mail jennifer.ortiz@bzh.uni-heidelberg.de
Marina Pelzl
TA

Lab:Room 122 / Phone: +49 6221 54-4336
Mail:marina.pelzl@bzh.uni-heidelberg.de

Auch im Raum 246 unter -4524 erreichbar!

 RoomPhone
LAB 122 +49 6221 54-4336
E-Mail marina.pelzl@bzh.uni-heidelberg.de
Jürgen Reichert
TA

Lab:Room 121 / Phone: +49 6221 54-4156
Office:Room 101 / Phone: +49 6221 54-4325
Mail:juergen.reichert@bzh.uni-heidelberg.de

 RoomPhone
LAB 121 +49 6221 54-4156
OFFICE 101 +49 6221 54-4325
E-Mail juergen.reichert@bzh.uni-heidelberg.de

Publications 


2010
Ebert AD, Laußmann M, Wegehingel S, Kaderali L, Erfle H, Reichert J, Lechner J, Beer HD, Pepperkok R, Nickel W. Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is essential for unconventional secretion.
Traffic 2010; 11(6):813-26.

2009
Ortiz J, Funk C, Schäfer A, Lechner J. Stu1 inversely regulates kinetochore capture and spindle stability.
Genes Dev. 2009; 23(23):2778-91.

Kemmler S, Stach M, Knapp M, Ortiz J, Pfannstiel J, Ruppert T, Lechner J. Mimicking Ndc80 phosphorylation triggers spindle assembly checkpoint signalling.
EMBO J. 2009; 28(8):1099-110.

2007
Maekawa H, Priest C, Lechner J, Pereira G, Schiebel E. The yeast centrosome translates the positional information of the anaphase spindle into a cell cycle signal.
J Cell Biol. 2007, 179(3):423-36.

2006
Sohn K, Schwenk J, Urban C, Lechner J, Schweikert M, Rupp S. Getting in touch with Candida albicans: the cell wall of a fungal pathogen.
Curr Drug Targets. 2006, 7(4):505-512.

Grosshans BL, Grötsch H, Mukhopadhyay D, Fernández IM, Pfannstiel J, Idrissi FZ, Lechner J, Riezman H, Geli MI. TEDS site phosphorylation of the yeast myosins I is required for ligand-induced but not for constitutive endocytosis of the G protein-coupled receptor Ste2p.
J Biol Chem. 2006, 281(16):11104-14.

2004
Kerres A, Vietmeier-Decker C, Ortiz J, Karig I, Beuter C, Hegemann J, Lechner J, Fleig U. The fission yeast kinetochore component Spc7 associates with the EB1 family member Mal3 and is required for kinetochore-spindle association.
Mol Biol Cell. 2004, 15(12):5255-67.

Rodriguez-Navarro S, Fischer T, Luo MJ, Antunez O, Brettschneider S, Lechner J, Perez-Ortin JE, Reed R, Hurt E. Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery.
Cell. 2004, 116(1):75-86.

2003
Seelenmeyer C, Wegehingel S, Lechner J, Nickel W. The cancer antigen CA125 represents a novel counter receptor for galectin-1.
J Cell Sci. 2003, 116(Pt 7):1305-18.

Milkereit P, Strauss D, Bassler J, Gadal O, Kühn H, Schütz S, Gas N, Lechner J, Hurt E, Tschochner H. A Noc complex specifically involved in the formation and nuclear export of ribosomal 40 S subunits.
J Biol Chem. 2003, 278(6):4072-81.

Scharfenberger M, Ortiz J, Grau N, Janke C, Schiebel E, Lechner J. Nsl1p is essential for the establishment of bipolarity and the localization of the Dam-Duo complex.
EMBO J. 2003, 22(24):6584-97.

2002
Fischer T, Sträßer K, Rácz A, Rodriguez-Navarro S, Oppizzi M, Ihrig P, Lechner J, Hurt E. The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores.
Embo J .2002, 21(21): 5843-5852.

Janke C, Ortíz J, Tanaka TU, Lechner J, Schiebel E. Four new subunits of the Dam1-Duo1 complex reveal novel functions in sister kinetochore biorientation. EMBO J. 2002, 21(1-2):181-93.

Stemmann O, Neidig A, Köcher T, Wilm M, Lechner J. Hsp90 enables Ctf13p/Skp1p to nucleate the budding yeast kinetochore.
Biochemistry 2002, 99(13):8585-90.

2001
Janke, C., Ortiz, J., Lechner, J., Shevchenko, A., Shevchenko, A., Magiera, M.M., Schramm, C., and Schiebel, E. 2001. The budding yeast proteins Spc24p and Spc25p interact with Ndc80p and Nuf2p at the kinetochore and are important for kinetochore clustering and checkpoint control.
The EMBO J. 20, 777-791

Bassler J, Grandi P, Gadal O, et al. Identification of a 60S preribosomal particle that is closely linked to nuclear export. Mol Cell 2001; 8:517-29.

Gommel DU, Memon AR, Heiss A, et al. Recruitment to Golgi membranes of ADP-ribosylation factor 1 is mediated by the cytoplasmic domain of p23. Embo J 2001; 20:6751-60.

2000
Hemmerich P, Stoyan T, Wieland G, Koch M, Lechner J, Diekmann S. Interaction of yeast kinetochore proteins with centromere- protein/transcription factor cbf1 [In Process Citation]. Proc Natl Acad Sci U S A 2000; 97:12583-8.

Ortiz J, Lechner J. The budding yeast kinetochore: less simple than expected. Protoplasma 2000; 211:12-19.

1999
Ortiz J, Stemmann O, Rank S, Lechner J. A putative protein complex consisting of Ctf19, Mcm21, and Okp1 represents a missing link in the budding yeast kinetochore. Genes Dev 1999; 13:1140-55.

Pietrasanta LI, Thrower D, Hsieh W, et al. Probing the Saccharomyces cerevisiae centromeric DNA (CEN DNA)-binding factor 3 (CBF3) kinetochore complex by using atomic force microscopy. Proc Natl Acad Sci U S A 1999; 96:3757-62.

Stoyan T, Eck R, Lechner J, Hemmerich P, Kunkel W, Diekmann S. Cloning of a centromere binding factor 3d (CBF3D) gene from Candida glabrata. Yeast 1999; 15:793-8.

1996
Lechner J, Ortiz J. The Saccharomyces cerevisiae kinetochore. FEBS Lett 1996; 389:70-4.

Stemmann O, Lechner J. The Saccharomyces cerevisiae kinetochore contains a cyclin-CDK complexing homologue, as identified by in vitro reconstitution. Embo J 1996; 15:3611-20.

1994
Lechner J. A zinc finger protein, essential for chromosome segregation, constitutes a putative DNA binding subunit of the Saccharomyces cerevisiae kinetochore complex, Cbf3. Embo J 1994; 13:5203-11.

1993
Jiang W, Lechner J, Carbon J. Isolation and characterization of a gene (CBF2) specifying a protein component of the budding yeast kinetochore. J Cell Biol 1993; 121:513-9.

Lechner J, Wieland F. Analysis of bacterial glycoproteins. Methods Mol Biol 1993; 14:119-29.

1991
Lechner J, Carbon J. A 240 kd multisubunit protein complex, CBF3, is a major component of the budding yeast centromere. Cell 1991; 64:717-25.

1989
Lechner J, Wieland F. Structure and biosynthesis of prokaryotic glycoproteins. Annu Rev Biochem 1989; 58:173-94.

1987
Lechner J, Sumper M. The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria. J Biol Chem 1987; 262:9724-9.

1986
Wieland F, Lechner J, Sumper M. Iduronic acid is a constituent of sulfated dolichyl phosphate oligosaccharides in halobacteria. FEBS Lett. 1986; 195:77-81.

Wieland F, Lechner J, Sumper M. Sulfated Dolicholphosphate Oligosaccharides are Transiently Methylated during Biosynthesis of Halobacterial Glycoproteins. System. Appl. Microbiol. 1986; 7:286-392.

1985
Lechner J, Wieland F, Sumper M. Biosynthesis of sulfated saccharides N-glycosidically linked to the protein via glucose. Purification and identification of sulfated dolichyl monophosphoryl tetrasaccharides from halobacteria. J Biol Chem 1985; 260:860-6.

Lechner J, Wieland F, Sumper M. Transient methylation of dolichyl oligosaccharides is an obligatory step in halobacterial sulfated glycoprotein biosynthesis. J Biol Chem 1985; 260:8984-9.

1982
Wieland F, Lechner J, Sumper M. The Cell Wall Glycoprotein of Halobacteria: Structural, Functional and Biosynthetiv Aspects. Zentralbl. Bacteriol. Mikrobiol. Hyg. 1982; 1 Abt. Orig. C 3,:161-170.

1981
Wieland F, Lechner J, Bernhardt G, Sumper M. Sulfation of a repetitive saccharide in halobacterial cell wall glycoprotein. FEBS Lett 1981; 132:319-323.


Collaborations 


Dr. Elmar Schiebel
Cancer Research UK Paterson Laboratories
Christie Hospital NHS Trust
Wilmslow Road
Manchester M20 4BX
UK

Funding 


DFG Einzelantrag

Contact



Heidelberg University
Biochemistry Center (BZH)
Im Neuenheimer Feld 328
69120 Heidelberg

Office:
+49 6221 54-4371
Lab:
+49 6221 54-5424
Fax:
+49 6221 54-5586
E-Mail:
johannes.lechner@bzh.uni-heidelberg.de


LOGO Biochemizentrum Heidelberg Heidelberg University Biochemistry Center (BZH)
Im Neuenheimer Feld 328
69120 Heidelberg
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  • Sinning
  • Söllner
  • Wieland
  • Former Research Groups »
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