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Originally published In Press as doi:10.1074/jbc.M101707200 on April 13, 2001

J. Biol. Chem., Vol. 276, Issue 24, 20973-20980, June 15, 2001
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Coactivator p300 Acetylates the Interferon Regulatory Factor-2 in U937 Cells following Phorbol Ester Treatment*

Atsuko MasumiDagger § and Keiko Ozato

From the Dagger  Department of Safety Research on Biologics, National Institute of Infectious Diseases, Tokyo 208-0011, Japan and  Laboratory of Molecular Growth Regulation, NICHD, National Institutes of Health, Bethesda, Maryland 20892

Interferon regulatory factor-2 (IRF-2) is a transcription factor of the IRF family that represses interferon-mediated gene expression. In the present study, we show that human monocytic U937 cells express truncated forms of IRF-2 containing the DNA binding domain but lacking much of the C-terminal regulatory domain. U937 cells are shown to respond to phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) to induce expression of histone acetylases p300 and p300/CBP-associated factor (PCAF). In addition, TPA treatment led to the appearance of full-length IRF-2, along with a reduction of the truncated protein. Interestingly, full-length IRF-2 in TPA-treated U937 cells occurred as a complex with p300 as well as PCAF and was itself acetylated. Consistent with these results, recombinant IRF-2 was acetylated by p300 and to a lesser degree by PCAF in vitro. Another IRF member, IRF-1, an activator of interferon-mediated transcription, was also acetylated in vitro by these acetylases. Finally, we demonstrate that the addition of IRF-2 but not IRF-1 inhibits core histone acetylation by p300 in vitro. The addition of IRF-2 also inhibited acetylation of nucleosomal histones in TPA-treated U937 cells. Acetylated IRF-2 may affect local chromatin structure in vivo by inhibiting core histone acetylation and may serve as a mechanism by which IRF-2 negatively regulates interferon-inducible transcription.

* This work was supported in part by the Ministry of Health Science and Welfare of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Safety Research on Biologics, 4-7-1, Gakuen, Musashimurayama-shi, National Institute of Infectious Diseases, Tokyo, Japan. Tel.: 81-425-61-0771; Fax: 81-425-65-3315; E-mail: amasumi@nih.go.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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