Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro

doi:10.1042/BJ20141437

	Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro
	Li, Hong-Tao 1; Gong, Ting 1; Zhou, Zhen 1; Liu, Yu-Ting 1; Cao, Xiongwen 1; He, Yongning 1; Chen, Charlie Degui 1; Zhou, Jin-Qiu1,2
	2015-05
发表期刊	BIOCHEMICAL JOURNAL (IF:4.4[JCR-2023],3.7[5-Year])
ISSN	0264-6021
卷号	467 页码:507-515
发表状态	已发表
DOI	10.1042/BJ20141437
摘要	Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate protein arginine residues. PRMTs' substrates include histones and a variety of non-histone proteins. Previous studies have shown that yeast Hmt1 is a type I PRMT and methylates histone H4 arginine 3 and several mRNA-binding proteins. Hmt1 forms dimers or oligomers, but how dimerization or oligomerization affects its activity remains largely unknown. We now report that Hmt1 can methylate histone H3 arginine 2 (H3R2) in vitro. The dimerization but not hexamerization is essential for Hmt1's activity. Interestingly, the methyltransferase activity of Hmt1 on histone H3R2 requires reciprocal contributions from two Hmt1 molecules. Our results suggest an intermolecular trans-complementary mechanism by which Hmt1 dimer methylates its substrates.
关键词	arginine methyltransferase dimer Hmt1 histone H3R2 yeast
收录类别	SCI
语种	英语
资助项目	Postdoctoral Fellowship Program of Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences[2011KIP503]
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
WOS记录号	WOS:000353217200013
出版者	PORTLAND PRESS LTD
WOS关键词	CRYSTAL-STRUCTURE ; METHYLATION ; METHYLTRANSFERASE ; INSIGHTS ; DNA ; IDENTIFICATION ; EXPRESSION ; PATHWAY ; COMPLEX ; SYSTEM
原始文献类型	Article
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/2217
专题	生命科学与技术学院_特聘教授组_周金秋组
通讯作者	Chen, Charlie Degui
作者单位	1.Univ Chinese Acad Sci, Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, State Key Lab Mol Biol,Shanghai Inst Biol Sci, Shanghai 200031, Peoples R China 2.Shanghai Tech Univ, Sch Life Sci & Technol, Shanghai 200031, Peoples R China
推荐引用方式 GB/T 7714	Li, Hong-Tao,Gong, Ting,Zhou, Zhen,et al. Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro[J]. BIOCHEMICAL JOURNAL,2015,467:507-515.
APA	Li, Hong-Tao.,Gong, Ting.,Zhou, Zhen.,Liu, Yu-Ting.,Cao, Xiongwen.,...&Zhou, Jin-Qiu.(2015).Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro.BIOCHEMICAL JOURNAL,467,507-515.
MLA	Li, Hong-Tao,et al."Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro".BIOCHEMICAL JOURNAL 467(2015):507-515.