期刊
JOURNAL OF CELL SCIENCE
卷 131, 期 13, 页码 -出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.214924
关键词
Cohesin; DNA repair; Mitosis; Meiosis; Schizosaccharomyces pombe
类别
资金
- Vedecka Grantova Agentura MSVVaS SR a SAV (Slovak Grant Agency
- VEGA) [1/0196/14, 1/0450/18]
- Agentura na Podporu Vyskumu a Vyvoja (Slovak Research and Development Agency
- APPV) [APVV-0334-12]
- Austrian Science Fund (FWF) [P30516, P21437, W1238, F34]
- ERA-CAPS [I 3686]
- European Community's Seventh Framework Programme (FP7/2007-2013) [PCIG11-GA-2012-322300]
- People Programme (Marie Curie Actions) European Union's Seventh Framework Programme [REA] [609427, 0032/01/02]
- Slovak Academy of Sciences, VEGA [2/0026/18, 2/0070/16]
- Slovak Research and Development Agency [APVV-0111-12, APVV-16-0120]
- People Programme (Marie Curie Actions) of the EU FP7 under REA [0070/01/02]
- Austrian Science Fund (FWF) [W1238] Funding Source: Austrian Science Fund (FWF)
The canonical role of cohesin is to mediate sister chromatid cohesion. In addition, cohesin plays important roles in processes such as DNA repair and regulation of gene expression. Mounting evidence suggests that various post-translational modifications, including phosphorylation, acetylation and sumoylation regulate cohesin functions. Our mass spectrometry analysis of cohesin purified from Schizosaccharomyces pombe cells revealed that the cohesin subunit Psm1 is methylated on two evolutionarily conserved lysine residues, K536 and K1200. We found that mutations that prevent methylation of Psm1 K536 and K1200 render sensitivity to DNA-damaging agents and show positive genetic interactions with mutations in genes encoding the Mus81-Eme1 endonuclease. Yeast two-hybrid and co-immunoprecipitation assays showed that there were interactions between subunits of the cohesin and Mus81-Eme1 complexes. We conclude that cohesin is methylated and that mutations that prevent methylation of Psm1 K536 and K1200 show synthetic phenotypes with mutants defective in the homologous recombination DNA repair pathway.
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