2005 Fiscal Year Final Research Report Summary
Analysis of a novel coactivator that activates the c-fos gene
| Project/Area Number |
16570148
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Molecular biology
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| Research Institution | University of Tsukuba (2005)
Saitama Medical University (2004) |
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Principal Investigator |
HISATAKE Koji University of Tsukuba, Graduate School of Comprehensive Human Sciences, Professor, 大学院・人間総合科学研究科, 教授 (70271236)
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| Co-Investigator(Kenkyū-buntansha) |
NAKADAI Tomoyoshi Saitama Medical School, Department of Medicine, Research associate, 医学部, 助手 (10364770)
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| Project Period (FY) |
2004 – 2005
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| Keywords | transcription factor / coactivator / TFIID / baculovirus / activator / basal transcriptional machinery |
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| Research Abstract |
We have studied on the transcriptional activity of ILF2/ILF3. The primary structures of ILF2/ILF3 suggested that these factors might bind double-stranded RNA and be involved in the defense against viral infection. We performed a detailed analysis of the interaction of ILF3 with PKR and found that while ILF3 bound the phosphorylated form of PKR, it failed to interact with non-phosphorylated form of PKR. We also found that double-stranded RNA reduced the interactions of ILF3 with activators including SRF, Elk-1, ATF1 and CREB. The reduction in the interactions was not observed with the mutant ILF3 that lacked dsRNA-binding ability, indicating the direct requirement of dsRNA binding in reducing the interactions. Together, the results suggested that the altered transcription of the c-fos gene by dsRNA involve dynamic changes in the complex formation between ILF3/ILF2 and the activators. Furthermore, in vitro transcription studies showed that dsRNA attenuated transcription of the c-fos gene, indicating a negative feedback effect on c-fos transcription by its own transcript. Interaction studied revealed novel interactions between ILF2/ILF3 and PRMT1, PRMT2 and PRMT5. As these proteins methylate arginine residues in proteins, the presence of these interactions supported a view that transcription of the c-fos gene is regulated by methylation of arginine residued with the histone molecules.
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Research Products
(4 results)
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[Journal Article] The fission yeast protein, Kerlp, is an ortholog of RNA polymerase I subunit A14 in Saccharomyces cerevisiae, and is required for stable association of Rm3p and RPA21 in Pol2005
Author(s)
Imazawa Y, Hisatake K, Mitsuzawa H, Matsumoto M, Tsukui T, Nakagawa K, Nakadai T, Shimada M, Ishihama A, Nogi Y
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Journal Title
J. Biol. Chem 280・12
Pages: 11467-11474
Description
「研究成果報告書概要(和文)」より
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[Journal Article] The fission yeast protein, Ker1p, is an ortholog of RNA polymerase I subunit A14 in Saccharomyces cerevisiae, and is required for stable association of Rrn3p and RPA21 in Pol2005
Author(s)
Imazawa Y, Hisatake K, Mitsuzawa H, Matsumoto M, Tsukui T, Nakagawa K, Nakadai T, Shimada M, Ishihama A, Nogi Y
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Journal Title
Journal of Biochemistry 280(12)
Pages: 11467-11474
Description
「研究成果報告書概要(欧文)」より
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