Nature2014-06-26 3:53 PM

一个组蛋白变体的伴侣分子 ANP32E is a histone chaperone that removes H2A.Z from chromatin

论文摘要 

组蛋白H2A.Z是组蛋白H2A(真核细胞的染色质中所存在的标准组蛋白之一)的一个变体。H2A.Z在转录和其他细胞核过程中有重要功能。在这篇论文中,Ali Hamiche及同事发现人蛋白ANP32E是一个H2A.Z伴侣,能够促使H2A.Z从染色质中被清除。生化和结构数据指出了ANP32E识别和驱赶H2A.Z的分子基础,而全基因组图谱分析则揭示了ANP32E是怎样调控H2A.Z在基因组重要调控区域中之存在的。

Abstract 

H2A.Z is an essential histone variant implicated in the regulation of key nuclear events. However, the metazoan chaperones responsible for H2A.Z deposition and its removal from chromatin remain unknown. Here we report the identification and characterization of the human protein ANP32E as a specific H2A.Z chaperone. We show that ANP32E is a member of the presumed H2A.Z histone-exchange complex p400/TIP60. ANP32E interacts with a short region of the docking domain of H2A.Z through a new motif termed H2A.Z interacting domain (ZID). The 1.48 Å resolution crystal structure of the complex formed between the ANP32E-ZID and the H2A.Z/H2B dimer and biochemical data support an underlying molecular mechanism for H2A.Z/H2B eviction from the nucleosome and its stabilization by ANP32E through a specific extension of the H2A.Z carboxy-terminal α-helix. Finally, analysis of H2A.Z localization in ANP32E−/− cells by chromatin immunoprecipitation followed by sequencing shows genome-wide enrichment, redistribution and accumulation of H2A.Z at specific chromatin control regions, in particular at enhancers and insulators.

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