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首页> 外文期刊>Journal of Molecular Biology >Histone H4 K16Q mutation, an acetylation mimic, causes structural disorder of its n-terminal basic patch in the nucleosome
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Histone H4 K16Q mutation, an acetylation mimic, causes structural disorder of its n-terminal basic patch in the nucleosome

机译：组蛋白H4 K16Q突变，一种乙酰化模拟物，导致其核小体n端基本补丁的结构异常

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Histone tails and their posttranslational modifications play important roles in regulating the structure and dynamics of chromatin. For histone H4, the basic patch K 16R 17H 18R 19 in the N-terminal tail modulates chromatin compaction and nucleosome sliding catalyzed by ATP-dependent ISWI chromatin remodeling enzymes while acetylation of H4 K16 affects both functions. The structural basis for the effects of this acetylation is unknown. Here, we investigated the conformation of histone tails in the nucleosome by solution NMR. We found that backbone amides of the N-terminal tails of histones H2A, H2B, and H3 are largely observable due to their conformational disorder. However, only residues 1-15 in H4 can be detected, indicating that residues 16-22 in the tails of both H4 histones fold onto the nucleosome core. Surprisingly, we found that K16Q mutation in H4, a mimic of K16 acetylation, leads to a structural disorder of the basic patch. Thus, our study suggests that the folded structure of the H4 basic patch in the nucleosome is important for chromatin compaction and nucleosome remodeling by ISWI enzymes while K16 acetylation affects both functions by causing structural disorder of the basic patch K 16R 17H 18R 19.
机译：组蛋白尾巴及其翻译后修饰在调节染色质的结构和动力学中起重要作用。对于组蛋白H4，N末端尾巴中的基本补丁K 16R 17H 18R 19调节由ATP依赖性ISWI染色质重塑酶催化的染色质紧实和核小体滑动，而H4 K16的乙酰化影响这两个功能。这种乙酰化作用的结构基础是未知的。在这里，我们通过溶液NMR研究了核小体中组蛋白尾巴的构象。我们发现组蛋白H2A，H2B和H3的N末端尾部的骨架酰胺由于其构象障碍而在很大程度上可观察到。但是，只能检测到H4中的残基1-15，这表明两个H4组蛋白尾巴中的残基16-22都折叠到核小体核心上。出乎意料的是，我们发现H4中的K16Q突变（模仿K16乙酰化）导致基本斑块的结构紊乱。因此，我们的研究表明，核小体中H4基本斑块的折叠结构对于ISWI酶的染色质压实和核小体重塑很重要，而K16乙酰化会通过引起基本斑块K 16R 17H 18R 19的结构紊乱而影响两种功能。

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