High mobility group proteins and their post-translational modifications

被引:71
|
作者
Zhang, Qingchun [1 ]
Wang, Yinsheng [1 ]
机构
[1] Univ Calif Riverside, Dept Chem, Riverside, CA 92521 USA
来源
基金
美国国家卫生研究院;
关键词
high mobility group protein; post-translational modification; mass spectrometry;
D O I
10.1016/j.bbapap.2008.04.028
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 high mobility group (HMG) proteins, including HMGA, HMGB and HMGN, are abundant and ubiquitous nuclear proteins that bind to DNA, nucleosome and other multi-protein complexes in a dynamic and reversible fashion to regulate DNA processing in the context of chromatin. All HMG proteins, like histone proteins, are subjected to extensive post-translational modifications (PTMs), such as lysine acetylation, arginine/lysine methylation and serine/threonine phosphorylation, to modulate their interactions with DNA and other proteins. There is a growing appreciation for the complex relationship between the PTMs of HMG proteins and their diverse biological activities. Here, we reviewed the identified covalent modifications of HMG proteins, and highlighted how these PTMs affect the functions of HMG proteins in a variety of cellular processes. (c) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:1159 / 1166
页数:8
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