Histone H3 tail modifications regulate structure and dynamics of the H1 C-terminal domain within nucleosomes.
Histone H3 tail modifications regulate structure and dynamics of the H1 C-terminal domain within nucleosomes.
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组蛋白 H3 尾部修饰调节核小体内 H1 C 末端结构域的结构和动态。
DOI：
10.1101/2023.05.11.540398
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发表时间：
2023
期刊：
影响因子：
--
通讯作者：
Hayes,JeffreyJ
中科院分区：
文献类型：
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作者：
Das,SubhraKanti;Kumar,Ashok;Hao,Fanfan;DiPiazza,AmberRCutter;Lee,Tae-Hee;Hayes,JeffreyJ
尽管连接物组蛋白H1s很重要，但它们如何在染色质中相互作用，特别是高度正电荷和内在无序的H1 C末端结构域(CTD)如何结合和稳定核小体和高阶染色质结构仍不清楚。使用单分子FRET我们发现，在H1-核小体复合体中，大约一半的H1CTD表现出明确的FRET值，表明不同的静态构象，而其余的群体表现出动态变化的值，类似于在没有核小体的情况下观察到的H1。我们还发现，CTD的前30个残基参与了与连接DNA的第一个∼20bp的相对局域性相互作用，并且CTD中的两个独立区域参与了依赖H1的连接DNA的组织，这与一些非随机的CTD-连接DNA相互作用是一致的。最后，我们的数据表明，组蛋白H3尾部的乙酰化模拟诱导了核小体结合的H1 CTD的解缩和增强的动力学。(148字)
Despite their importance, how linker histone H1s interact in chromatin and especially how the highly positively charged and intrinsically disordered H1 C-terminal domain (CTD) binds and stabilizes nucleosomes and higher-order chromatin structures remains unclear. Using single-molecule FRET we found that about half of the H1 CTDs in H1-nucleosome complexes exhibit well-defined FRET values indicative of distinct, static conformations, while the remainder of the population exhibits dynamically changing values, similar to that observed for H1 in the absence of nucleosomes. We also find that the first 30 residues of the CTD participate in relatively localized interactions with the first ∼20 bp of linker DNA, and that two separate regions in the CTD contribute to H1-dependent organization of linker DNA, consistent with some non-random CTD-linker DNA interactions. Finally, our data show that acetylation mimetics within the histone H3 tail induce decondensation and enhanced dynamics of the nucleosome-bound H1 CTD. (148 words)