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核小体中的组蛋白尾部网络和调节。

Histone tail network and modulation in a nucleosome.

机构信息

Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.

Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan; Graduate School of Integrated Sciences for Life, Hiroshima University, 1-4-4 Kagamiyama, Higashi-Hiroshima 739-8528, Japan.

出版信息

Curr Opin Struct Biol. 2022 Aug;75:102436. doi: 10.1016/j.sbi.2022.102436. Epub 2022 Jul 18.

DOI:10.1016/j.sbi.2022.102436
PMID:35863166
Abstract

The structural unit of eukaryotic chromatin is a nucleosome, comprising two histone H2A/H2B heterodimers and one histone (H3/H4) tetramer, wrapped around by ∼146-bp core DNA and linker DNA. Flexible histone tails sticking out from the core undergo posttranslational modifications that are responsible for various epigenetic functions. Recently, the functional dynamics of histone tails and their modulation within the nucleosome and nucleosomal complexes have been investigated by integrating NMR, molecular dynamics simulations, and cryo-electron microscopy approaches. In particular, recent NMR studies have revealed correlations in the structures of histone N-terminal tails between H2A and H2B, as well as between H3 and H4 depending on linker DNA, suggesting that histone tail networks exist even within the nucleosome.

摘要

真核染色质的结构单元是核小体,由两个组蛋白 H2A/H2B 异二聚体和一个组蛋白(H3/H4)四聚体组成,核心 DNA 约 146bp 并缠绕着连接 DNA。从核心伸出的灵活组蛋白尾巴经历翻译后修饰,这些修饰负责各种表观遗传功能。最近,通过整合 NMR、分子动力学模拟和冷冻电镜方法,研究了组蛋白尾巴的功能动力学及其在核小体和核小体复合物中的调节。特别是,最近的 NMR 研究揭示了组蛋白 N 端尾巴在 H2A 和 H2B 之间,以及 H3 和 H4 之间的结构相关性,具体取决于连接 DNA,这表明组蛋白尾巴网络甚至存在于核小体中。

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