Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-8958
Science August 3, 2001; 293 (5531): 853-7.
Show Gene links Show Anatomy links

Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor.

Wang H , Huang ZQ , Xia L , Feng Q , Erdjument-Bromage H , Strahl BD , Briggs SD , Allis CD , Wong J , Tempst P , Zhang Y .


Abstract
Acetylation of core histone tails plays a fundamental role in transcription regulation. In addition to acetylation, other posttranslational modifications, such as phosphorylation and methylation, occur in core histone tails. Here, we report the purification, molecular identification, and functional characterization of a histone H4-specific methyltransferase PRMT1, a protein arginine methyltransferase. PRMT1 specifically methylates arginine 3 (Arg 3) of H4 in vitro and in vivo. Methylation of Arg 3 by PRMT1 facilitates subsequent acetylation of H4 tails by p300. However, acetylation of H4 inhibits its methylation by PRMT1. Most important, a mutation in the S-adenosyl-l-methionine-binding site of PRMT1 substantially crippled its nuclear receptor coactivator activity. Our finding reveals Arg 3 of H4 as a novel methylation site by PRMT1 and indicates that Arg 3 methylation plays an important role in transcriptional regulation.

PubMed ID: 11387442
Article link: Science
Grant support: [+]

Species referenced: Xenopus
Genes referenced: crebbp h4c4 prmt1