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Phospho-regulation of the Shugoshin - Condensin interaction at the centromere in budding yeast.
PLOS Genetics ( IF 4.5 ) Pub Date : 2020-08-18 , DOI: 10.1371/journal.pgen.1008569
Galal Yahya 1, 2 , Yehui Wu 3 , Karolina Peplowska 3, 4 , Jennifer Röhrl 3 , Young-Min Soh 5 , Frank Bürmann 6 , Stephan Gruber 5 , Zuzana Storchova 2
Affiliation  

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.



中文翻译:

出芽酵母中着丝粒处的Shugoshin-Condensin相互作用的磷酸调节。

姐妹染色单体与有丝分裂纺锤体之间正确的双向定向对于染色体分离至关重要。在发芽的酵母中,保守的蛋白质Shugoshin(Sgo1)通过募集蛋白质磷酸酶PP2A-Rts1和缩合蛋白复合物至着丝粒来促进生物定向。使用肽印迹,我们确定了Sgo1的丝氨酸丰富基序(SRM),它介导与凝缩蛋白的相互作用,对于着丝粒凝缩蛋白的募集和生物定向的建立是必不可少的。我们表明相互作用是通过SRM内的磷酸化来调节的,并且我们使用质谱法确定了磷酸位点。磷酸化和耐磷酸化突变体的分析表明,SRM磷酸化破坏了Shugoshin-condensin的相互作用。我们提供证据表明Mps1是纺锤体装配检查点中的中心激酶,直接将SRM中的Sgo1磷酸化,以调节与凝聚素的相互作用,从而使凝聚素定位于着丝粒。我们的发现确定了控制发芽酵母中着丝粒处的守护甜心活性的新机制。

更新日期:2020-08-19
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