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Interferon regulatory factor-7 synergizes with other transcription factors through multiple interactions with p300/CBP coactivators.

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.

Pubmed ID: 12604599 RIS Download

Mesh terms: Amino Acid Sequence | Animals | Cell Line | DNA | DNA-Binding Proteins | Humans | Interferon Regulatory Factor-3 | Interferon Regulatory Factor-7 | Molecular Sequence Data | Nuclear Proteins | Protein Conformation | Proto-Oncogene Proteins c-jun | Rabbits | Structure-Activity Relationship | Trans-Activators | Transcription Factors | Transcriptional Activation | Virus Activation

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Associated grants

  • Agency: NIAID NIH HHS, Id: AI 20642

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