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Nucleosome eviction in mitosis assists condensin loading and chromosome condensation

机译:在有丝分裂中驱逐核小体有助于凝缩蛋白上样和染色体凝结

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摘要

Condensins associate with DNA and shape mitotic chromosomes. Condensins are enriched nearby highly expressed genes during mitosis, but how this binding is achieved and what features associated with transcription attract condensins remain unclear. Here, we report that condensin accumulates at or in the immediate vicinity of nucleosome‐depleted regions during fission yeast mitosis. Two transcriptional coactivators, the Gcn5 histone acetyltransferase and the RSC chromatin‐remodelling complex, bind to promoters adjoining condensin‐binding sites and locally evict nucleosomes to facilitate condensin binding and allow efficient mitotic chromosome condensation. The function of Gcn5 is closely linked to condensin positioning, since neither the localization of topoisomerase II nor that of the cohesin loader Mis4 is altered in gcn5 mutant cells. We propose that nucleosomes act as a barrier for the initial binding of condensin and that nucleosome‐depleted regions formed at highly expressed genes by transcriptional coactivators constitute access points into chromosomes where condensin binds free genomic DNA.
机译:凝缩蛋白与DNA结合并塑造有丝分裂染色体。凝集素在有丝分裂期间富集了附近的高表达基因,但是如何实现这种结合以及与转录相关的哪些特征吸引凝缩蛋白尚不清楚。在这里,我们报道凝缩蛋白在裂殖酵母有丝分裂过程中聚集在核小体耗尽的区域或附近。 Gcn5组蛋白乙酰基转移酶和RSC染色质重塑复合体是两个转录共激活因子,它们与邻接凝缩蛋白结合位点的启动子结合并局部清除核小体,以促进凝缩蛋白结合并允许有效的有丝分裂染色体凝缩。 Gcn5的功能与凝集素的定位紧密相关,因为拓扑异构酶II的定位和黏附素装载剂Mis4的定位在gcn5突变细胞中均未改变。我们建议核小体充当凝集素初始结合的屏障,并且转录共激活因子在高度表达的基因上形成的核小体耗尽区域构成凝集素结合自由基因组DNA的染色体的访问点。

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