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A more recent version of this article appeared on March 31, 2006
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M511093200v1
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Papers In Press, published online ahead of print February 4, 2006
J. Biol. Chem, 10.1074/jbc.M511093200
Submitted on October 12, 2005
Accepted on February 4, 2006

Histone H3 lysine 9 methyltransferase G9a is a transcriptional coactivator for nuclear receptors

David Y. Lee, Jeffrey P. Northrop, Min-Hao Kuo, and Michael R. Stallcup

Dept of Biochemistry & Molecular Biology, Univ of Southern California, Los Angeles, CA 90089-9151

Corresponding Author: stallcup{at}usc.edu

Methylation of Lys-9 of histone H3 has been associated with repression of transcription. G9a is a histone H3 Lys-9 methyltransferase localized in euchromatin and acts as a corepressor for specific transcription factors. Here we demonstrate that G9a also functions as a coactivator for nuclear receptors, cooperating synergistically with nuclear receptor coactivators GRIP1, CARM1, and p300 in transient transfection assays. This synergy depends strongly on the arginine-specific protein methyltransferase activity of CARM1 but does not absolutely require the enzymatic activity of G9a and is specific to CARM1 and G9a among various protein methyltransferases. Reduction of endogenous G9a diminished hormonal activation of an endogenous target gene by the androgen receptor, and G9a associates with regulatory regions of this same gene. G9a fused to Gal4 DNA binding domain can repress transcription in a lysine methyltransferase-dependent manner; however, the histone modifications associated with transcriptional activation can inhibit the methyltransferase activity of G9a. These findings suggest a link between histone arginine and lysine methylation and a mechanism for controlling whether G9a functions as a corepressor or coactivator.


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