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首页> 外文期刊>Journal of Molecular Biology >The PHD and chromo domains regulate the atpase activity of the human chromatin remodeler CHD4
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The PHD and chromo domains regulate the atpase activity of the human chromatin remodeler CHD4

机译：PHD和染色体域调节人类染色质重塑剂CHD4的atpase活性

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摘要

The NuRD (nucleosome remodeling and deacetylase) complex serves as a crucial epigenetic regulator of cell differentiation, proliferation, and hematopoietic development by coupling the deacetylation and demethylation of histones, nucleosome mobilization, and the recruitment of transcription factors. The core nucleosome remodeling function of the mammalian NuRD complex is executed by the helicase-domain-containing ATPase CHD4 (Mi-2β) subunit, which also contains N-terminal plant homeodomain (PHD) and chromo domains. The mode of regulation of chromatin remodeling by CHD4 is not well understood, nor is the role of its PHD and chromo domains. Here, we use small-angle X-ray scattering, nucleosome binding ATPase and remodeling assays, limited proteolysis, cross-linking, and tandem mass spectrometry to propose a three-dimensional structural model describing the overall shape and domain interactions of CHD4 and discuss the relevance of these for regulating the remodeling of chromatin by the NuRD complex.
机译：通过结合组蛋白的去乙酰化和去甲基化，核小体动员以及转录因子的募集，NuRD（核小体重塑和脱乙酰基酶）复合物成为细胞分化，增殖和造血发育的关键表观遗传调节剂。哺乳动物NuRD复合体的核心核小体重塑功能由含有解旋酶结构域的ATPase CHD4（Mi-2β）亚基执行，该亚基还包含N端植物同源结构域（PHD）和染色体结构域。通过CHD4调节染色质重塑的模式尚不完全清楚，其PHD和染色体结构域的作用也不甚了解。在这里，我们使用小角度X射线散射，核小体结合ATPase和重塑分析，有限的蛋白水解，交联和串联质谱法，提出了描述CHD4整体形状和结构域相互作用的三维结构模型，并讨论了这些与通过NuRD复合物调节染色质重塑的相关性。

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