Gayatri Sitaram, Bedford Mark T
Department of Molecular Carcinogenesis, The University of Texas MD Anderson Cancer Center, Smithville, TX 78957, USA.
Department of Molecular Carcinogenesis, The University of Texas MD Anderson Cancer Center, Smithville, TX 78957, USA.
Biochim Biophys Acta. 2014 Aug;1839(8):702-10. doi: 10.1016/j.bbagrm.2014.02.015. Epub 2014 Feb 28.
Arginine methylation is a common posttranslational modification (PTM) that alters roughly 0.5% of all arginine residues in the cells. There are three types of arginine methylation: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA), and symmetric dimethylarginine (SDMA). These three PTMs are enriched on RNA-binding proteins and on histones, and also impact signal transduction cascades. To date, over thirty arginine methylation sites have been cataloged on the different core histones. These modifications alter protein structure, impact interactions with DNA, and also generate docking sites for effector molecules. The primary "readers" of methylarginine marks are Tudor domain-containing proteins. The complete family of thirty-six Tudor domain-containing proteins has yet to be fully characterized, but at least ten bind methyllysine motifs and eight bind methylarginine motifs. In this review, we will highlight the biological roles of the Tudor domains that interact with arginine methylated motifs, and also address other types of interactions that are regulated by these particular PTMs. This article is part of a Special Issue entitled: Molecular mechanisms of histone modification function.
精氨酸甲基化是一种常见的翻译后修饰（PTM），它改变了细胞中约0.5%的所有精氨酸残基。精氨酸甲基化有三种类型：单甲基精氨酸（MMA）、不对称二甲基精氨酸（ADMA）和对称二甲基精氨酸（SDMA）。这三种PTM在RNA结合蛋白和组蛋白上富集，也影响信号转导级联反应。迄今为止，已在不同的核心组蛋白上编目了三十多个精氨酸甲基化位点。这些修饰改变蛋白质结构，影响与DNA的相互作用，还为效应分子生成对接位点。甲基精氨酸标记的主要“读取器”是含Tudor结构域的蛋白质。包含36个含Tudor结构域的蛋白质的完整家族尚未完全表征，但至少有10个结合甲基赖氨酸基序，8个结合甲基精氨酸基序。在本综述中，我们将重点介绍与精氨酸甲基化基序相互作用的Tudor结构域的生物学作用，并讨论由这些特定PTM调节的其他类型的相互作用。本文是名为：组蛋白修饰功能的分子机制的特刊的一部分。
