NuA4核心复合物通过双重识别机理乙酰化核小体组蛋白H4  

The NuA4 Core Complex Acetylates Nucleosomal Histone H4 through a Double Recognition Mechanism

作　　者：Peng Xu Chengmin Li Zhihong Chen Shuanying Jiang Shilong Fan Jiawei Wang Junbiao Dai 朱平[2] 陈柱成 

机构地区：[1]不详 [2]中科院生物物理所 [3]清华大学生命科学学院

出　　处：《科学新闻》2017年第4期88-88,共1页Science News

基　　金：国家自然科学基金委员会;科技部;中组部;中科院等项目的经费支持

摘　　要：NuA4催化核小体组蛋白H4的乙酰化是一个广为人知的表观遗传学现象，在酵母中参与调控多种基因组过程。在这个工作中，本研究报道了NuA4核心复合物的晶体结构以及结合核小体的电子显微镜结构。这些结构表明，乙酰转移酶的组蛋白结合口袋发生重排，暗示了该酶的一种激活机理。NuA4 catalyzes the acetylation of nucleosomes at histone H4, which is a well-established epigenetic event, controlling many genomic processes in Saccharomyces 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 amodifying enzyme in the context of the nucleosome.

关 键 词：蛋白 复合 识别 晶体结构 表观遗传学 电子显微镜 激活机理 基因组 

分 类 号：Q510.3[生物学—生物化学]