{"title":"非必要的动点核蛋白通过类波罗激酶促进减数分裂染色体的凝聚。","authors":"Deepika Trakroo, Prakhar Agarwal, Anushka Alekar, Santanu Kumar Ghosh","doi":"10.1091/mbc.E24-08-0348","DOIUrl":null,"url":null,"abstract":"<p><p>Chromosome condensation plays a pivotal role during faithful chromosome segregation, hence, understanding the factors that drive condensation is crucial to get mechanistic insight into chromosome segregation. Previously, we showed that in budding yeast, the absence of the nonessential kinetochore proteins affects chromatin-condensin association in meiosis but not in mitosis. A differential organization of the kinetochores, that we and others observed earlier during mitosis and meiosis may contribute to the meiotic-specific role. Here, with our in-depth investigation using in vivo chromosome condensation assays in cells lacking a nonessential kinetochore protein, Ctf19, we establish that these proteins have roles in achieving a higher meiotic condensation without influencing much of the mitotic condensation. We further observed an accumulation of the polo-like kinase Cdc5 owing to its higher protein stability in <i>ctf19Δ</i> meiotic cells. High Cdc5 activity causes hyperphosphorylation of the condensin resulting in its reduced stability and concomitant decreased association with the chromatin. Overall, our findings highlight the role of Ctf19 in promoting meiotic chromosome condensation by influencing the activity of Cdc5 and thereby affecting the stability and association of condensin with the chromatin.</p>","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar14"},"PeriodicalIF":3.1000,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11809314/pdf/","citationCount":"0","resultStr":"{\"title\":\"Nonessential kinetochore proteins contribute to meiotic chromosome condensation through polo-like kinase.\",\"authors\":\"Deepika Trakroo, Prakhar Agarwal, Anushka Alekar, Santanu Kumar Ghosh\",\"doi\":\"10.1091/mbc.E24-08-0348\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Chromosome condensation plays a pivotal role during faithful chromosome segregation, hence, understanding the factors that drive condensation is crucial to get mechanistic insight into chromosome segregation. Previously, we showed that in budding yeast, the absence of the nonessential kinetochore proteins affects chromatin-condensin association in meiosis but not in mitosis. A differential organization of the kinetochores, that we and others observed earlier during mitosis and meiosis may contribute to the meiotic-specific role. Here, with our in-depth investigation using in vivo chromosome condensation assays in cells lacking a nonessential kinetochore protein, Ctf19, we establish that these proteins have roles in achieving a higher meiotic condensation without influencing much of the mitotic condensation. We further observed an accumulation of the polo-like kinase Cdc5 owing to its higher protein stability in <i>ctf19Δ</i> meiotic cells. High Cdc5 activity causes hyperphosphorylation of the condensin resulting in its reduced stability and concomitant decreased association with the chromatin. Overall, our findings highlight the role of Ctf19 in promoting meiotic chromosome condensation by influencing the activity of Cdc5 and thereby affecting the stability and association of condensin with the chromatin.</p>\",\"PeriodicalId\":18735,\"journal\":{\"name\":\"Molecular Biology of the Cell\",\"volume\":\" \",\"pages\":\"ar14\"},\"PeriodicalIF\":3.1000,\"publicationDate\":\"2025-02-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11809314/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Molecular Biology of the Cell\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1091/mbc.E24-08-0348\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2024/12/20 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q3\",\"JCRName\":\"CELL BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Molecular Biology of the Cell","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1091/mbc.E24-08-0348","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/12/20 0:00:00","PubModel":"Epub","JCR":"Q3","JCRName":"CELL BIOLOGY","Score":null,"Total":0}
Nonessential kinetochore proteins contribute to meiotic chromosome condensation through polo-like kinase.
Chromosome condensation plays a pivotal role during faithful chromosome segregation, hence, understanding the factors that drive condensation is crucial to get mechanistic insight into chromosome segregation. Previously, we showed that in budding yeast, the absence of the nonessential kinetochore proteins affects chromatin-condensin association in meiosis but not in mitosis. A differential organization of the kinetochores, that we and others observed earlier during mitosis and meiosis may contribute to the meiotic-specific role. Here, with our in-depth investigation using in vivo chromosome condensation assays in cells lacking a nonessential kinetochore protein, Ctf19, we establish that these proteins have roles in achieving a higher meiotic condensation without influencing much of the mitotic condensation. We further observed an accumulation of the polo-like kinase Cdc5 owing to its higher protein stability in ctf19Δ meiotic cells. High Cdc5 activity causes hyperphosphorylation of the condensin resulting in its reduced stability and concomitant decreased association with the chromatin. Overall, our findings highlight the role of Ctf19 in promoting meiotic chromosome condensation by influencing the activity of Cdc5 and thereby affecting the stability and association of condensin with the chromatin.
期刊介绍:
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