组蛋白的翻译后修饰（PTMs），如乙酰化、甲基化、磷酸化和泛素化（遍在蛋白化），在染色质的动力学调节中发挥重要的作用。组蛋白上各种修饰的组合（常称为“组蛋白密码”）在表观遗传调控水平上进一步丰富了DNA遗传密码的信息含量。而非组蛋白上的翻译后修饰能够调节蛋白质之间的相互作用、稳定性、细胞内定位和（或）酶的活性。蛋白质的磷酸化、泛素化、乙酰化已经得到广泛的研究，然而只有很小部分研究报道非组蛋白也可以通过赖氨酸残基的甲基化实现翻译后修饰。本文综述了非组蛋白赖氨酸甲基化研究的发展现状。和磷酸化和乙酰化一样，赖氨酸甲基化也是一种不可缺少的翻译后修饰，在细胞活动过程中有着重要的作用。

图例: p53翻译后修饰

Lysine methylation: beyond histones

Xi Zhang, Hong Wen, and Xiaobing Shi

Department of Biochemistry & Molecular Biology, University of Texas MD Anderson Cancer Center, Houston, 77030, USA.

Posttranslational modifications (PTMs) ofhistone proteins, such as acetylation, methylation, phosphorylation, andubiquitylation, play essential roles in regulating chromatin dynamics.Combinations of different modifications on the histone proteins, termed'histone code' in many cases, extend the information potential of the geneticcode by regulating DNA at the epigenetic level. Many PTMs occur on non-histoneproteins as well as histones, regulating protein-protein interactions,stability, localization, and/or enzymatic activities of proteins involved indiverse cellular processes. Although protein phosphorylation, ubiquitylation,and acetylation have been extensively studied, only a few proteins other thanhistones have been reported that can be modified by lysine methylation. Thisreview summarizes the current progress on lysine methylation of non-histoneproteins, and we propose that lysine methylation, like phosphorylation andacetylation, is a common PTM that regulates proteins in diverse cellular processes.

Acta Biochim Biophys Sin (Shanghai). 2012 Jan;44(1):14-27. doi: 10.1093/abbs/gmr100.

全文: http://abbs.oxfordjournals.org/content/44/1/14.full.pdf+html