Analyses of virus-induced homomeric and heteromeric protein associations between IRF-3 and coactivator CBP/p300
| Autor: | Keiko Tamura, Hideo Namiki, Saburo Aimoto, Shoko Yoshimura, Tomokatsu Iwamura, Mitsutoshi Yoneyama, Wakako Suhara, Takashi Fujita |
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| Rok vydání: | 2000 |
| Předmět: |
Phosphopeptides
Interferon Regulatory Factor-7 Newcastle disease virus Biology Biochemistry Binding Competitive Cell Line Serine Mice Coactivator Homomeric Animals Point Mutation Nuclear protein Phosphorylation Molecular Biology Transcription factor Phosphopeptide Nuclear Proteins General Medicine Precipitin Tests Cell biology DNA-Binding Proteins Trans-Activators Interferon Regulatory Factor-3 E1A-Associated p300 Protein Interferon regulatory factors Transcription Factors |
| Zdroj: | ResearcherID |
| ISSN: | 0021-924X |
| Popis: | Cellular genes including the type I interferon genes are activated in response to viral infection. We previously reported that IRF-3 (interferon regulatory factor 3) is specifically phosphorylated on serine residues and directly transmits a virus-induced signal from the cytoplasm to the nucleus, and then participates in the primary phase of gene induction. In this study, we analyzed the molecular mechanism of IRF-3 activation further. The formation of a stable homomeric complex of IRF-3 between the specifically phosphorylated IRF-3 molecules occurred. While virus-induced IRF-7 did not bind to p300, the phosphorylated IRF-3 complex formed a stable multimeric complex with p300 (active holocomplex). Competition using a synthetic phosphopeptide corresponding to the activated IRF-3 demonstrated that p300 directly recognizes the structure in the vicinity of the phosphorylated residues of IRF-3. These results indicated that the phosphorylation of serine residues at positions 385 and 386 is critical for the formation of the holocomplex, presumably through a conformational switch facilitating homodimer formation and the generation of the interaction interface with CBP/p300. |
| Databáze: | OpenAIRE |
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