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组蛋白尾部构象:与 DNA 的模糊关系。

Histone Tail Conformations: A Fuzzy Affair with DNA.

机构信息

Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.

Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.

出版信息

Trends Biochem Sci. 2021 Jul;46(7):564-578. doi: 10.1016/j.tibs.2020.12.012. Epub 2021 Feb 4.

DOI:10.1016/j.tibs.2020.12.012
PMID:33551235
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8195839/
Abstract

The core histone tails are critical in chromatin structure and signaling. Studies over the past several decades have provided a wealth of information on the histone tails and their interaction with chromatin factors. However, the conformation of the histone tails in a chromatin relevant context has remained elusive. Only recently has enough evidence emerged to start to build a structural model of the tails in the context of nucleosomes and nucleosome arrays. Here, we review these studies and propose that the histone tails adopt a high-affinity fuzzy complex with DNA, characterized by robust but dynamic association. Furthermore, we discuss how these DNA-bound conformational ensembles promote distinct chromatin structure and signaling, and that their fuzzy nature is important in transitioning between functional states.

摘要

核心组蛋白尾部在染色质结构和信号转导中起着关键作用。在过去几十年的研究中,人们获得了大量关于组蛋白尾部及其与染色质因子相互作用的信息。然而,在与染色质相关的环境中,组蛋白尾部的构象仍然难以捉摸。直到最近,才出现了足够的证据来开始构建核小体和核小体阵列中尾部的结构模型。在这里,我们回顾了这些研究,并提出组蛋白尾部与 DNA 形成高亲和力的模糊复合物,其特征是稳健但动态的结合。此外,我们还讨论了这些与 DNA 结合的构象集合如何促进不同的染色质结构和信号转导,以及它们的模糊性质在功能状态之间的转换中是很重要的。

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本文引用的文献

1
Nucleosome composition regulates the histone H3 tail conformational ensemble and accessibility.核小体组成调节组蛋白 H3 尾部构象整体和可及性。
Nucleic Acids Res. 2021 May 7;49(8):4750-4767. doi: 10.1093/nar/gkab246.
2
Acetylated histone H4 tail enhances histone H3 tail acetylation by altering their mutual dynamics in the nucleosome.乙酰化组蛋白 H4 尾部通过改变核小体中它们的相互动态,增强了组蛋白 H3 尾部的乙酰化。
Proc Natl Acad Sci U S A. 2020 Aug 18;117(33):19661-19663. doi: 10.1073/pnas.2010506117. Epub 2020 Aug 3.
3
Dual protease type XIII/pepsin digestion offers superior resolution and overlap for the analysis of histone tails by HX-MS.双蛋白酶 XIII/胃蛋白酶消化为通过 HX-MS 分析组蛋白尾部提供了更好的分辨率和重叠性。
Methods. 2020 Dec 1;184:135-140. doi: 10.1016/j.ymeth.2020.01.016. Epub 2020 Jan 28.
4
Dynamics of the nucleosomal histone H3 N-terminal tail revealed by high precision single-molecule FRET.高精度单分子 FRET 揭示核小体组蛋白 H3 N 端尾部的动力学
Nucleic Acids Res. 2020 Feb 20;48(3):1551-1571. doi: 10.1093/nar/gkz1186.
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Organization of Chromatin by Intrinsic and Regulated Phase Separation.染色质的固有和调控相分离组织。
Cell. 2019 Oct 3;179(2):470-484.e21. doi: 10.1016/j.cell.2019.08.037. Epub 2019 Sep 19.
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Histone chaperone exploits intrinsic disorder to switch acetylation specificity.组蛋白伴侣利用固有无序性来切换乙酰化特异性。
Nat Commun. 2019 Aug 6;10(1):3435. doi: 10.1038/s41467-019-11410-7.
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Molecular recognition of nucleosomes by binding partners.结合蛋白对核小体的分子识别。
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Biophysics of Chromatin Dynamics.染色质动力学的生物物理学。
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ACS Chem Biol. 2019 Apr 19;14(4):579-586. doi: 10.1021/acschembio.8b01049. Epub 2019 Mar 12.