组蛋白乙酰化抑制 RSC 并稳定+1 核小体。
Histone Acetylation Inhibits RSC and Stabilizes the +1 Nucleosome.
机构信息
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
出版信息
Mol Cell. 2018 Nov 1;72(3):594-600.e2. doi: 10.1016/j.molcel.2018.09.030. Epub 2018 Oct 25.
Abstract
The +1 nucleosome of yeast genes, within which reside transcription start sites, is characterized by histone acetylation, by the displacement of an H2A-H2B dimer, and by a persistent association with the RSC chromatin-remodeling complex. Here we demonstrate the interrelationship of these characteristics and the conversion of a nucleosome to the +1 state in vitro. Contrary to expectation, acetylation performs an inhibitory role, preventing the removal of a nucleosome by RSC. Inhibition is due to both enhanced RSC-histone interaction and diminished histone-chaperone interaction. Acetylation does not prevent all RSC activity, because stably bound RSC removes an H2A-H2B dimer on a timescale of seconds in an irreversible manner.
摘要
酵母基因的+1 核小体（其中包含转录起始位点）的特征是组蛋白乙酰化、H2A-H2B 二聚体的置换以及与 RSC 染色质重塑复合物的持续关联。在这里，我们证明了这些特征的相互关系以及核小体在体外向+1 状态的转化。与预期相反，乙酰化起到抑制作用，阻止 RSC 去除核小体。抑制作用既源于增强的 RSC-组蛋白相互作用，也源于减弱的组蛋白伴侣相互作用。乙酰化并不能阻止所有的 RSC 活性，因为稳定结合的 RSC 会以不可逆的方式在数秒内去除 H2A-H2B 二聚体。
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