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	Identification and characterization of two closely related histone h4 arginine 3 methyltransferases in arabidopsis thaliana
	Yan, Dongsheng; Zhang, Yong; Niu, Lifang; Yuan, Yi; Cao, Xiaofeng
刊名	Biochemical journal
	2007-11-15
卷号	408页码:113-121
关键词	Arabidopsis thaliana Arginine methylation Fibrillarin 2 Histone modification Protein arginine n-methyltransferase (prmt) Rna methyltransferase
ISSN号	0264-6021
DOI	10.1042/bj20070786
通讯作者	Cao, xiaofeng(xfcao@genetics.ac.cn)
英文摘要	Arginine methylation of histone h3 and h4 plays important roles in transcriptional regulation in eukaryotes such as yeasts, fruitflies, nematode worms, fish and mammals; however, less is known in plants. in the present paper, we report the identification and characterization of two arabidopsis thaliana protein arginine n-methyltransferases, atprmt1a and atprmt1b, which exhibit high homology with human prmt1. both atprmt1a and atprmt1b methylated histone h4, h2a, and myelin basic protein in vitro. site-directed mutagenesis of the third arginine (r3) on the n-terminus of histone h4 to lysine (h4r3n) completely abolished the methylation of histone h4. when fused to gfp (green fluorescent protein), both methyltransferases localized to the cytoplasm as well as to the nucleus. consistent with their subcellular distribution, gst (glutathione transferase) pull-down assays revealed an interaction between the two methyltransferases, suggesting that both proteins may act together in a functional unit. in addition, we demonstrated that atfib2 (arabidopsis thaliana fibrillarin 2), an rna methyltransferase, is a potential substrate for atprmt1a and atprmt1b, and, furthermore, uncovered a direct interaction between the protein methyltransferase and the rna methyltransferase. taken together, our findings implicate atprmt1a and atprmt1b as h4-r3 protein arginine n-methyltransferases in arabidopsis and may be involved in diverse biological processes inside and outside the nucleus.
WOS关键词	RIBOSOMAL-RNA METHYLATION ; N-METHYLTRANSFERASE ; IN-VIVO ; SUBSTRATE-SPECIFICITY ; TRANSCRIPTIONAL ACTIVATION ; PROTEIN METHYLTRANSFERASE ; SUBCELLULAR-LOCALIZATION ; H2A UBIQUITINATION ; GENE DUPLICATION ; DNA METHYLATION
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
语种	英语
出版者	PORTLAND PRESS LTD
WOS记录号	WOS:000250951800013
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2381801
专题	中国科学院大学
通讯作者	Cao, Xiaofeng
作者单位	1.Chinese Acad Sci, Ctr Plant Gene Res, Natl Key Lab plant Genom, Beijing 100101, Peoples R China 2.Grad Univ Chinese Acad Sci, Beijing 100039, Peoples R China
推荐引用方式 GB/T 7714	Yan, Dongsheng,Zhang, Yong,Niu, Lifang,et al. Identification and characterization of two closely related histone h4 arginine 3 methyltransferases in arabidopsis thaliana[J]. Biochemical journal,2007,408:113-121.
APA	Yan, Dongsheng,Zhang, Yong,Niu, Lifang,Yuan, Yi,&Cao, Xiaofeng.(2007).Identification and characterization of two closely related histone h4 arginine 3 methyltransferases in arabidopsis thaliana.Biochemical journal,408,113-121.
MLA	Yan, Dongsheng,et al."Identification and characterization of two closely related histone h4 arginine 3 methyltransferases in arabidopsis thaliana".Biochemical journal 408(2007):113-121.

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