Suppr超能文献

组蛋白 H3 尾部乙酰化通过多种机制调节 ATP 依赖的重塑。

Histone H3 tail acetylation modulates ATP-dependent remodeling through multiple mechanisms.

机构信息

Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901-4413, USA.

出版信息

Nucleic Acids Res. 2011 Oct;39(19):8378-91. doi: 10.1093/nar/gkr535. Epub 2011 Jul 11.

Abstract

There is a close relationship between histone acetylation and ATP-dependent chromatin remodeling that is not fully understood. We show that acetylation of histone H3 tails affects SWI/SNF (mating type switching/ sucrose non fermenting) and RSC (remodels structure of chromatin) remodeling in several distinct ways. Acetylation of the histone H3 N-terminal tail facilitated recruitment and nucleosome mobilization by the ATP-dependent chromatin remodelers SWI/SNF and RSC. Tetra-acetylated H3, but not tetra-acetylated H4 tails, increased the affinity of RSC and SWI/SNF for nucleosomes while also changing the subunits of SWI/SNF that interact with the H3 tail. The enhanced recruitment of SWI/SNF due to H3 acetylation is bromodomain dependent, but is not further enhanced by additional bromodomains found in RSC. The combined effect of H3 acetylation and transcription activators is greater than either separately which suggests they act in parallel to recruit SWI/SNF. Besides enhancing recruitment, H3 acetylation increased nucleosome mobilization and H2A/H2B displacement by RSC and SWI/SNF in a bromodomain dependent manner and to a lesser extent enhanced ATP hydrolysis independent of bromodomains. H3 and H4 acetylation did not stimulate disassembly of adjacent nucleosomes in short arrays by SWI/SNF or RSC. These data illustrate how histone acetylation modulates RSC and SWI/SNF function, and provide a mechanistic insight into their collaborative efforts to remodel chromatin.

摘要

组蛋白乙酰化与 ATP 依赖的染色质重塑之间存在密切关系,但目前尚未完全了解。我们发现组蛋白 H3 尾部的乙酰化以几种不同的方式影响着 SWI/SNF(交配型转换/蔗糖非发酵)和 RSC(重塑染色质结构)重塑。组蛋白 H3 N 端尾部的乙酰化促进了 ATP 依赖的染色质重塑因子 SWI/SNF 和 RSC 的募集和核小体运动。四乙酰化的 H3,但不是四乙酰化的 H4 尾部,增加了 RSC 和 SWI/SNF 对核小体的亲和力,同时也改变了与 H3 尾部相互作用的 SWI/SNF 亚基。由于 H3 乙酰化而增强的 SWI/SNF 募集依赖于溴结构域,但不会被 RSC 中发现的额外溴结构域进一步增强。由于 H3 乙酰化和转录激活因子的联合效应大于任何一种单独的效应,这表明它们以平行的方式募集 SWI/SNF。除了增强募集作用外,H3 乙酰化还以溴结构域依赖的方式增强了 RSC 和 SWI/SNF 对核小体的动员和 H2A/H2B 置换作用,并且在一定程度上增强了与溴结构域无关的 ATP 水解。H3 和 H4 乙酰化并没有刺激 SWI/SNF 或 RSC 对短阵列中相邻核小体的解体。这些数据说明了组蛋白乙酰化如何调节 RSC 和 SWI/SNF 的功能,并为它们协同重塑染色质的机制提供了深入的了解。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验