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本文引用的文献

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Histone H4 Tails in Nucleosomes: a Fuzzy Interaction with DNA.核小体中的组蛋白 H4 尾部:与 DNA 的模糊相互作用。
Angew Chem Int Ed Engl. 2021 Mar 15;60(12):6480-6487. doi: 10.1002/anie.202012046. Epub 2021 Feb 12.
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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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The conformation of the histone H3 tail inhibits association of the BPTF PHD finger with the nucleosome.组蛋白 H3 尾部的构象抑制了 BPTF PHD 指与核小体的结合。
Elife. 2018 Apr 12;7:e31481. doi: 10.7554/eLife.31481.
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Chromatin Higher-Order Folding: A Perspective with Linker DNA Angles.染色质高级折叠:以连接 DNA 角度看问题。
Biophys J. 2018 May 22;114(10):2290-2297. doi: 10.1016/j.bpj.2018.03.009. Epub 2018 Apr 6.
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Site-Specific Studies of Nucleosome Interactions by Solid-State NMR Spectroscopy.通过固态 NMR 光谱学进行核小体相互作用的位点特异性研究。
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Accessibility of the histone H3 tail in the nucleosome for binding of paired readers.核小体组蛋白 H3 尾部结合配对读取器的可达性。
Nat Commun. 2017 Nov 14;8(1):1489. doi: 10.1038/s41467-017-01598-x.
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Topological diversity of chromatin fibers: Interplay between nucleosome repeat length, DNA linking number and the level of transcription.染色质纤维的拓扑多样性:核小体重复长度、DNA连接数与转录水平之间的相互作用。
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Insights into Nucleosome Organization in Mouse Embryonic Stem Cells through Chemical Mapping.通过化学图谱深入了解小鼠胚胎干细胞中的核小体组织
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Modulations of DNA Contacts by Linker Histones and Post-translational Modifications Determine the Mobility and Modifiability of Nucleosomal H3 Tails.连接组蛋白和翻译后修饰对DNA接触的调控决定了核小体H3尾巴的流动性和可修饰性。
Mol Cell. 2016 Jan 21;61(2):247-59. doi: 10.1016/j.molcel.2015.12.015. Epub 2016 Jan 14.
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Subnucleosomal structures and nucleosome asymmetry across a genome.全基因组范围内的亚核小体结构与核小体不对称性
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染色质中组蛋白H3尾巴的构象动力学

Conformational Dynamics of Histone H3 Tails in Chromatin.

作者信息

Zandian Mohamad, Gonzalez Salguero Nicole, Shannon Matthew D, Purusottam Rudra N, Theint Theint, Poirier Michael G, Jaroniec Christopher P

机构信息

Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States.

Department of Physics, The Ohio State University, Columbus, Ohio 43210, United States.

出版信息

J Phys Chem Lett. 2021 Jul 8;12(26):6174-6181. doi: 10.1021/acs.jpclett.1c01187. Epub 2021 Jun 29.

DOI:10.1021/acs.jpclett.1c01187
PMID:34184895
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8788308/
Abstract

Chromatin is a supramolecular DNA-protein complex that compacts eukaryotic genomes and regulates their accessibility and functions. Dynamically disordered histone H3 N-terminal tails are among key chromatin regulatory components. Here, we used high-resolution-magic-angle-spinning NMR measurements of backbone amide N spin relaxation rates to investigate, with residue-specific detail, the dynamics and interactions of H3 tails in recombinant C,N-enriched nucleosome arrays containing 15, 30, or 60 bp linker DNA between the nucleosome repeats. These measurements were compared to analogous data available for mononucleosomes devoid of linker DNA or containing two 20 bp DNA overhangs. The H3 tail dynamics in nucleosome arrays were found to be considerably attenuated compared with nucleosomes with or without linker DNA due to transient electrostatic interactions with the linker DNA segments and the structured chromatin environment. Remarkably, however, the H3 tail dynamics were not modulated by the specific linker DNA length within the 15-60 bp range investigated here.

摘要

染色质是一种超分子DNA-蛋白质复合物,它压缩真核生物基因组并调节其可及性和功能。动态无序的组蛋白H3 N端尾巴是关键的染色质调节成分之一。在这里,我们使用 backbone amide N 自旋弛豫率的高分辨率魔角旋转核磁共振测量,以残基特异性细节研究了在核小体重复序列之间含有15、30或60 bp连接子DNA的重组C、N富集核小体阵列中H3尾巴的动力学和相互作用。这些测量结果与不含连接子DNA或含有两个20 bp DNA突出端的单核小体的类似数据进行了比较。由于与连接子DNA片段和结构化染色质环境的瞬时静电相互作用,发现核小体阵列中的H3尾巴动力学与有或没有连接子DNA的核小体相比有相当程度的减弱。然而,值得注意的是,在这里研究的15-60 bp范围内,H3尾巴动力学并未受到特定连接子DNA长度的调节。