Histone arginine methylation

被引：350

作者：

Di Lorenzo, Alessandra ^{[1
]}

Bedford, Mark T. ^{[1
]}

机构：

[1] Univ Texas MD Anderson Canc Ctr, Div Sci Pk Res, Smithville, TX 78957 USA

来源：

FEBS LETTERS | 2011年 / 585卷 / 13期

关键词：

Arginine methylation; Histone code; Tudor domain; CARM1; ChIP-seq; ESTROGEN-RECEPTOR-ALPHA; N-METHYLTRANSFERASE; SUBSTRATE-SPECIFICITY; GENE-EXPRESSION; PROTEIN METHYLTRANSFERASE; SYMMETRIC DIMETHYLARGININE; TRANSCRIPTIONAL ACTIVATION; MASS-SPECTROMETRY; CRYSTAL-STRUCTURE; STRUCTURAL BASIS;

D O I：

10.1016/j.febslet.2010.11.010

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：

Arginine methylation is a common posttranslational modification (PTM). This type of PTM occurs on both nuclear and cytoplasmic proteins, and is particularly abundant on shuttling proteins. In this review, we will focus on one aspect of this PTM: the diverse roles that arginine methylation of the core histone tails play in regulating chromatin function. A family of nine protein arginine methyltransferases (PRMTs) catalyze methylation reactions, and a subset target histones. Importantly, arginine methylation of histone tails can promote or prevent the docking of key transcriptional effector molecules, thus playing a central role in the orchestration of the histone code. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：2024 / 2031

页数：8

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