Litt Michael, Qiu Yi, Huang Suming
Medical Education Center, Ball State University, Muncie, IN 47302, USA.
Biosci Rep. 2009 Apr;29(2):131-41. doi: 10.1042/BSR20080176.
PRMTs (protein arginine N-methyltransferases) specifically modify the arginine residues of key cellular and nuclear proteins as well as histone substrates. Like lysine methylation, transcriptional repression or activation is dependent upon the site and type of arginine methylation on histone tails. Recent discoveries imply that histone arginine methylation is an important modulator of dynamic chromatin regulation and transcriptional controls. However, under the shadow of lysine methylation, the roles of histone arginine methylation have been under-explored. The present review focuses on the roles of histone arginine methylation in the regulation of gene expression, and the interplays between histone arginine methylation, histone acetylation, lysine methylation and chromatin remodelling factors. In addition, we discuss the dynamic regulation of arginine methylation by arginine demethylases, and how dysregulation of PRMTs and their activities are linked to human diseases such as cancer.
蛋白质精氨酸N-甲基转移酶(PRMTs)特异性修饰关键细胞和核蛋白以及组蛋白底物的精氨酸残基。与赖氨酸甲基化一样,转录抑制或激活取决于组蛋白尾部精氨酸甲基化的位点和类型。最近的发现表明,组蛋白精氨酸甲基化是动态染色质调控和转录控制的重要调节因子。然而,在赖氨酸甲基化的影响下,组蛋白精氨酸甲基化的作用尚未得到充分研究。本综述重点关注组蛋白精氨酸甲基化在基因表达调控中的作用,以及组蛋白精氨酸甲基化、组蛋白乙酰化、赖氨酸甲基化和染色质重塑因子之间的相互作用。此外,我们还讨论了精氨酸去甲基酶对精氨酸甲基化的动态调控,以及PRMTs及其活性的失调如何与癌症等人类疾病相关联。