The NuA4 Core Complex Acetylates Nucleosomal Histone H4 through a Double Recognition Mechanism.
The NuA4 Core Complex Acetylates Nucleosomal Histone H4 through a Double Recognition Mechanism.
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NuA4 核心复合物通过双重识别机制乙酰化核小体组蛋白 H4
DOI：
10.1016/j.molcel.2016.07.024
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发表时间：
2016
期刊：
影响因子：
--
通讯作者：
Chen Zhucheng
中科院分区：
文献类型：
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作者：
Xu Peng;Li Chengmin;Chen Zhihong;Jiang Shuanying;Fan Shilong;Wang Jiawei;Dai Junbiao;Zhu Ping;Chen Zhucheng
NuA 4催化组蛋白H4处核小体的乙酰化，这是一个公认的表观遗传事件，控制着酿酒酵母中的许多基因组过程。在这里，我们报告的NuA 4核心复合物的晶体结构和冷冻电子显微镜结构的核小体。结构表明，酶的组蛋白结合口袋重排，表明其激活。该酶主要通过目标赖氨酸残基结合组蛋白尾部，优先选择-1位的小残基。该复合物在皿表面接合核小体，并将其催化口袋定位在靠近H4尾的位置，以实现选择性乙酰化。结合的数据揭示了一个空间序列的双重识别机制的组蛋白尾部的修饰酶的背景下的核小体。
NuA4 catalyzes the acetylation of nucleosomes at histone H4, which is a well-established epigenetic event, controlling many genomic processes inSaccharomyces cerevisiae. Here we report the crystal structures of the NuA4 core complex and a cryoelectron microscopy structure with the nucleosome. The structures show that the histone-binding pocket of the enzyme is rearranged, suggesting its activation. The enzyme binds the histone tail mainly through the target lysine residue, with a preference for a small residue at the −1 position. The complex engages the nucleosome at the dish face and orients its catalytic pocket close to the H4 tail to achieve selective acetylation. The combined data reveal a space-sequence double recognition mechanism of the histone tails by a modifying enzyme in the context of the nucleosome.