Phospho-regulation of the Shugoshin - Condensin interaction at the centromere in budding yeast

English version

Autoři: Galal Yahya Metwaly ^aff001; Yehui Wu ^aff003; Karolina Peplowska ^aff003; Jennifer Röhrl ^aff003; Young-Min Soh ^aff005; Frank Bürmann ^aff006; Stephan Gruber ^aff005; Zuzana Storchova ^aff002; Galal Yahya ^aff001
Působiště autorů: Department of Microbiology and Immunology, School of Pharmacy, Zagazig University, Egypt ^aff001; Department of Microbiology and Immunology School of Pharmacy, Zagazig University, Egypt ^aff001; Department of Molecular Genetics, TU Kaiserlautern, Kaiserslautern, Germany ^aff002; Max Planck Institute of Biochemistry, Martinsried, Germany ^aff003; Genomics and Bioinformatics Shared Resource, University of Hawaii Cancer Center, Honolulu, United States of America ^aff004; Department of Fundamental Microbiology, UNIL-Sorge District, Lausanne, Switzerland ^aff005; MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom ^aff006
Vyšlo v časopise: Phospho-regulation of the Shugoshin - Condensin interaction at the centromere in budding yeast. PLoS Genet 16(8): e32767. doi:10.1371/journal.pgen.1008569
Kategorie: Research Article
doi: https://doi.org/10.1371/journal.pgen.1008569

Souhrn

Correct bioriented attachment of sister chromatids to the mitotic spindle is essential for chromosome segregation. In budding yeast, the conserved protein shugoshin (Sgo1) contributes to biorientation by recruiting the protein phosphatase PP2A-Rts1 and the condensin complex to centromeres. Using peptide prints, we identified a Serine-Rich Motif (SRM) of Sgo1 that mediates the interaction with condensin and is essential for centromeric condensin recruitment and the establishment of biorientation. We show that the interaction is regulated via phosphorylation within the SRM and we determined the phospho-sites using mass spectrometry. Analysis of the phosphomimic and phosphoresistant mutants revealed that SRM phosphorylation disrupts the shugoshin–condensin interaction. We present evidence that Mps1, a central kinase in the spindle assembly checkpoint, directly phosphorylates Sgo1 within the SRM to regulate the interaction with condensin and thereby condensin localization to centromeres. Our findings identify novel mechanisms that control shugoshin activity at the centromere in budding yeast.

Klíčová slova:

Centromeres – Chromosome structure and function – Immunoblotting – Mitosis – Phosphorylation – Saccharomyces cerevisiae – Yeast

Zdroje

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