Accessibility of the histone H3 tail in the nucleosome for binding of paired readers.
Accessibility of the histone H3 tail in the nucleosome for binding of paired readers.
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DOI：
10.1038/s41467-017-01598-x
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发表时间：
2017-11-14
影响因子：
16.6
通讯作者：
Kutateladze TG
中科院分区：
文献类型：
--
作者：
Gatchalian J;Wang X;Ikebe J;Cox KL;Tencer AH;Zhang Y;Burge NL;Di L;Gibson MD;Musselman CA;Poirier MG;Kono H;Hayes JJ;Kutateladze TG
组蛋白结合域或阅读器的组合多价接触通常介导染色质相关蛋白的定位和活性。一对阅读器，蛋白质CHD 4的PHD指，已被证明可以识别组蛋白H3尾。在这里，我们描述了一种机制，这些连接，但独立的读者结合到完整的核小体核心颗粒（NCP）。全面的NMR，化学反应性，分子动力学和荧光分析点核小体内组蛋白-DNA相互作用的关键作用，减少了NCP，核小体DNA中的H3尾的可及性，以及调节核小体和/或组蛋白结合活性的读者之间的连接体。我们发现，CHD 4的第二个PHD指启动核小体的招聘，但这两个PHD都需要改变NCP动力学。我们的研究结果揭示了一个独特的调节机制，配对的读者与核小体，提供了一个复杂的平衡之间的合作和个人活动的读者协会。染色质重塑剂CHD 4含有两个PHD指状阅读器结构域，其已显示双链识别H3组蛋白尾部。在这里，作者描述了PHD指与完整的核小体核心颗粒结合的机制，揭示了合作和个体相互作用。
Combinatorial polyvalent contacts of histone-binding domains or readers commonly mediate localization and activities of chromatin-associated proteins. A pair of readers, the PHD fingers of the protein CHD4, has been shown to bivalently recognize histone H3 tails. Here we describe a mechanism by which these linked but independent readers bind to the intact nucleosome core particle (NCP). Comprehensive NMR, chemical reactivity, molecular dynamics, and fluorescence analyses point to the critical roles of intra-nucleosomal histone-DNA interactions that reduce the accessibility of H3 tails in NCP, the nucleosomal DNA, and the linker between readers in modulating nucleosome- and/or histone-binding activities of the readers. We show that the second PHD finger of CHD4 initiates recruitment to the nucleosome, however both PHDs are required to alter the NCP dynamics. Our findings reveal a distinctive regulatory mechanism for the association of paired readers with the nucleosome that provides an intricate balance between cooperative and individual activities of the readers. The chromatin remodeller CHD4 contains two PHD finger reader domains that have been shown to bivalently recognize H3 histone tails. Here, the authors describe a mechanism by which the PHD fingers bind to the intact nucleosome core particle, revealing both cooperative and individual interactions.
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影响因子：
14.9
作者：
Klein BJ;Muthurajan UM;Lalonde ME;Gibson MD;Andrews FH;Hepler M;Machida S;Yan K;Kurumizaka H;Poirier MG;Côté J;Luger K;Kutateladze TG
通讯作者：
Kutateladze TG
DOI：
10.1126/science.1235532
发表时间：
2013-05-31
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Kato H;Jiang J;Zhou BR;Rozendaal M;Feng H;Ghirlando R;Xiao TS;Straight AF;Bai Y
通讯作者：
Bai Y
影响因子：
23.9
作者：
Hu, Guang;Wade, Paul A.
通讯作者：
Wade, Paul A.
影响因子：
4.4
作者：
JORGENSEN, WL;CHANDRASEKHAR, J;KLEIN, ML
通讯作者：
KLEIN, ML
影响因子：
15
作者：
Kato, Hidenori;Gruschus, James;Ghirlando, Rodolfo;Tjandra, Nico;Bai, Yawen
通讯作者：
Bai, Yawen