Principles of nucleosome recognition by chromatin factors and enzymes

被引：87

作者：

McGinty, Robert K. ^{[1
]}

Tan, Song ^{[2
]}

机构：

[1] Univ N Carolina, Eshelman Sch Pharm, Div Chem Biol & Med Chem, Chapel Hill, NC 27515 USA

[2] Penn State Univ, Ctr Eukaryot Gene Regulat, Dept Biochem & Mol Biol, University Pk, PA 16802 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2021年 / 71卷

基金：

美国国家卫生研究院;

关键词：

Nucleosome; Chromatin; Histone; Acidic patch; Arginine anchor; Structural biology; STRUCTURAL BASIS; CRYSTAL-STRUCTURE; CORE PARTICLE; COMPLEX; MECHANISMS; DYNAMICS; CGAS;

D O I：

10.1016/j.sbi.2021.05.006

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The recent torrent of structures of chromatin complexes determined by cryoelectron microscopy provides an opportunity to discern general principles for how chromatin factors and enzymes interact with their nucleosome substrate. We find that many chromatin proteins use a strikingly similar arginine anchor and variant arginine interactions to bind to the nucleosome acidic patch. We also observe that many chromatin proteins target the H3 and H2B histone fold a1-loop1 elbows and the H2B C-terminal helix on the nucleosomal histone face. These interactions with the histones can be complemented with interactions with and distortions of nucleosomal DNA.

引用

页码：16 / 26

页数：11

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