Regulation of Transcription by a Protein Methyltransferase

Author:

Chen Dagang1,Ma Han1,Hong Heng1,Koh Stephen S.1,Huang Shih-Ming1,Schurter Brandon T.2,Aswad Dana W.2,Stallcup Michael R.1

Affiliation:

1. Department of Pathology HMR 301, University of Southern California, 2011 Zonal Avenue, Los Angeles, CA 90033, USA.

2. Department of Biochemistry and Molecular Biology, University of California, Biosciences II, Room 3205, Irvine, CA 92697, USA.

Abstract

The p160 family of coactivators, SRC-1, GRIP1/TIF2, and p/CIP, mediate transcriptional activation by nuclear hormone receptors. Coactivator-associated arginine methyltransferase 1 (CARM1), a previously unidentified protein that binds to the carboxyl-terminal region of p160 coactivators, enhanced transcriptional activation by nuclear receptors, but only when GRIP1 or SRC-1a was coexpressed. Thus, CARM1 functions as a secondary coactivator through its association with p160 coactivators. CARM1 can methylate histone H3 in vitro, and a mutation in the putative S -adenosylmethionine binding domain of CARM1 substantially reduced both methyltransferase and coactivator activities. Thus, coactivator-mediated methylation of proteins in the transcription machinery may contribute to transcriptional regulation.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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