Histone arginine methylations: their roles in chromatin dynamics and transcriptional regulation

被引:69
作者
Litt, Michael [3 ]
Qiu, Yi [1 ,2 ]
Huang, Suming [1 ,4 ,5 ]
机构
[1] Univ Florida, Coll Med, Shands Canc Ctr, Gainesville, FL 32611 USA
[2] Univ Florida, Coll Med, Dept Anat & Cell Biol, Gainesville, FL 32611 USA
[3] Ball State Univ, Med Educ Ctr, Muncie, IN 47302 USA
[4] Univ Florida, Coll Med, Dept Biochem & Mol Biol, Gainesville, FL 32611 USA
[5] Univ Florida, Coll Med, Genet Inst, Gainesville, FL 32611 USA
基金
美国国家卫生研究院;
关键词
arginine demethylase; cancer; chromatin insulator; histone cross-talk; protein arginine N-methyltransferase (PRMT); transcriptional regulation; PROTEIN METHYLATION; PHOSPHATIDYLSERINE RECEPTOR; N-METHYLTRANSFERASE; IN-VITRO; PRMT1; BINDING; COACTIVATOR; EXPRESSION; SUBSTRATE; CARM1;
D O I
10.1042/BSR20080176
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
Synopsis 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.
引用
收藏
页码:131 / 141
页数:11
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