Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

被引:374
作者
Strahl, BD
Briggs, SD
Brame, CJ
Caldwell, JA
Koh, SS
Ma, H
Cook, RG
Shabanowitz, J
Hunt, DF
Stallcup, MR
Allis, CD [1 ]
机构
[1] Univ Virginia, Hlth Sci Ctr, Dept Biochem & Mol Genet, Charlottesville, VA 22908 USA
[2] Univ Virginia, Hlth Sci Ctr, Dept Chem & Pathol, Charlottesville, VA 22908 USA
[3] Univ So Calif, Dept Pathol, Los Angeles, CA 90089 USA
[4] Baylor Coll Med, Dept Immunol, Houston, TX 77030 USA
关键词
D O I
10.1016/S0960-9822(01)00294-9
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
Posttranslational modifications of histone amino termini play an important role in modulating chromatin structure and function [1-3], Lysine methylation of histones has been well documented [4, 5], and recently this modification has been linked to cellular processes involving gene transcription and heterochromatin assembly [6-9]. However, the existence of arginine methylation on histones has remained unclear. Recent discoveries of protein arginine methyltransferases, CARM1 and PRMT1, as transcriptional coactivators for nuclear receptors suggest that histones may be physiological targets of these enzymes as part of a poorly defined transcriptional activation pathway [10-12], Here we show by using mass spectrometry that histone H4, isolated from asynchronously growing human 293T cells, is methylated at arginine 3 (Arg-3) in vivo. In support, a novel antibody directed against histone H4 methylated at Arg-3 independently demonstrates the in vivo occurrence of this modification and reveals that H4 Arg-3 methylation is highly conserved throughout eukaryotes, Finally, we show that PRMT1 is the major, if not exclusive, H4 Arg-3 methyltransfase in human 293T cells. These findings suggest a role for arginine methylation of histones in the transcription process. (C) 2001 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:996 / 1000
页数:5
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