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Originally published In Press as doi:10.1074/jbc.M207484200 on October 8, 2002

J. Biol. Chem., Vol. 277, Issue 51, 49417-49421, December 20, 2002
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Acetylation of Interferon Regulatory Factor-7 by p300/CREB-binding Protein (CBP)-associated Factor (PCAF) Impairs its DNA Binding*

Alexandre CaillaudDagger §, Arun Prakash, Eric Smith, Atsuko Masumi||, Ara G. HovanessianDagger , David E. Levy, and Isabelle MariéDagger **

From the Dagger  Unité de Virologie et Immunologie Cellulaire, Institut Pasteur, 75724 Paris, France, the  Department of Pathology and Kaplan Comprehensive Cancer Center, New York University School of Medicine, New York, New York 10016, and the || National Institute of Infectious Diseases, Tokyo 208-0011, Japan

Interferon regulatory factor 7 (IRF7) is an interferon-inducible transcription factor required for induction of delayed early interferon alpha  genes and the onset of a potent antiviral state. After induction of IRF7 by autocrine interferon, latent IRF7 is activated by virus-induced phosphorylation on serine residues within the C-terminal regulatory domain. Although it is likely that IRF7 is subjected to a cascade of events responsible for regulating its biological activity, to date no mechanism other than phosphorylation has been reported to modulate IRF7 activity. Here, we report that IRF7 is acetylated in vivo by the histone acetyltransferases p300/CBP-associated factor (PCAF) and GCN5. The single lysine residue target for acetylation, lysine 92, is located in the DNA-binding domain and is conserved throughout the entire IRF family. Mutation of lysine 92 resulted in complete abolition of DNA binding ability. However, a mutant that cannot be acetylated by PCAF due to a change in the surrounding amino acid context of lysine 92 showed increased DNA binding and activity compared with wild type IRF7. Conversely, we showed that acetylated IRF7 displayed impaired DNA binding capability and that over-expression of PCAF led to decreased IRF7 activity. Together, our results strongly suggest that acetylation of lysine 92 negatively modulates IRF7 DNA binding.

* This work was supported in part by grants from the Association sur la Recherche contre le Cancer (ARC) (to I. M.), by Grant R01 A146503 from the National Institute of Health, and by Grant 9951033T from the American Heart Association.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.

§ Recipient of a fellowship from ARC.

** To whom correspondence should be addressed: Dept. of Pathology, New York University School of Medicine, 550 First Ave., MSB 556, New York, NY 10016. Tel.: 212-263-8705; Fax: 212-263-8211; E-mail: isabellemarie@hotmail.com.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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