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Histone Acetylation Not Stoichiometry Regulates Linker Histone Binding in Saccharomyces cerevisiae

机译:组蛋白乙酰化而不是化学计量调节酿酒酵母中的接头组蛋白结合。

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摘要

Linker histones play a fundamental role in shaping chromatin structure, but how their interaction with chromatin is regulated is not well understood. In this study, we used a combination of genetic and genomic approaches to explore the regulation of linker histone binding in the yeast, Saccharomyces cerevisiae. We found that increased expression of , the yeast linker histone, resulted in a severe growth defect, despite only subtle changes in chromatin structure. Further, this growth defect was rescued by mutations that increase histone acetylation. Consistent with this, genome-wide analysis of linker histone occupancy revealed an inverse correlation with histone tail acetylation in both yeast and mouse embryonic stem cells. Collectively, these results suggest that histone acetylation negatively regulates linker histone binding in S. cerevisiae and other organisms and provide important insight into how chromatin structure is regulated and maintained to both facilitate and repress transcription.
机译:接头组蛋白在塑造染色质结构中起着基本作用,但是人们对它们与染色质的相互作用如何调节尚不十分了解。在这项研究中,我们结合了遗传学和基因组学方法,探索了酵母酵母中对组蛋白结合的调控。我们发现,尽管染色质结构只有细微的变化,酵母接头组蛋白的表达增加仍导致严重的生长缺陷。此外,通过增加组蛋白乙酰化的突变挽救了这种生长缺陷。与此相一致的是,在全基因组范围内对接头组蛋白占有率的分析揭示了酵母和小鼠胚胎干细胞中组蛋白尾巴乙酰化的反相关关系。总的来说,这些结果表明组蛋白乙酰化负调控酿酒酵母和其他生物中的接头组蛋白结合,并为如何调节和维持染色质结构以促进和抑制转录提供重要的见识。

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