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Originally published In Press as doi:10.1074/jbc.M212940200 on February 25, 2003

J. Biol. Chem., Vol. 278, Issue 18, 15495-15504, May 2, 2003
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Interferon Regulatory Factor-7 Synergizes with Other Transcription Factors through Multiple Interactions with p300/CBP Coactivators*

Hongmei YangDagger , Charles H. Lin§, Gang MaDagger , Michael O. BaffiDagger , and Marc G. WatheletDagger ||

From the Dagger  Department of Molecular and Cellular Physiology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267-0576 and the § Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138

Interferon regulatory factor (IRF)-7 is activated in response to virus infection and stimulates the transcription of a set of cellular genes involved in host antiviral defense. The mechanism by which IRF-7 is activated and cooperates with other transcription factors is not fully elucidated. Activation of IRF-7 results from a conformational change triggered by the virus-dependent phosphorylation of its C terminus. This conformational change leads to dimerization, nuclear accumulation, DNA-binding, and transcriptional transactivation. Here we show that activation of IRF-7, like that of IRF-3, is dependent on modifications of two distinct sets of Ser/Thr residues. Moreover, we show that different virus-inducible cis-acting elements display requirements for specific IRFs. In particular, the virus-responsive element of the ISG15 gene promoter can be activated by either IRF-3 or IRF-7 alone, whereas the P31 element of the interferon-beta gene is robustly activated only when IRF-3, IRF-7, and the p300/CBP coactivators are all present. Furthermore, we find that IRF-7 interacts with four distinct regions of p300/CBP. These interactions not only stimulate the intrinsic transcriptional activity of IRF-7, but they are also indispensable for its ability to strongly synergize with other transcription factors, including c-Jun and IRF-3.

* This work was supported by a Dean Research Award (to M. G. W.) and National Institutes of Health Grant AI20642 (to T. Maniatis, Harvard University) during its initial phase.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.

Present address: Dept. of Pathology, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115.

|| To whom correspondence should be addressed: Dept. of Molecular and Cellular Physiology, University of Cincinnati College of Medicine, 231 Albert Sabin Way, Cincinnati, OH 45267-0576. Tel.: 513-558-4515; Fax: 513-558-5738; E-mail: marc.wathelet@uc.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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