| Project/Area Number |
14580657
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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 |
Functional biochemistry
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| Research Institution | Faculty of Medical Sciences, University of Fukui |
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Principal Investigator |
FURUKAWA Takako University of Fukui, Biomedical imaging Research Center, Associate Professor, 高エネルギー医学研究センター, 助教授 (00221557)
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| Project Period (FY) |
2002 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 2003: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 2002: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | chromatin remodeling / SWI / SNF / Osa / chromatin remodeling complex / 転写調節 |
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| Research Abstract |
We isolated two related but distinct cDNA clones, hOsa-1 and hOsa-2, the 1argest component of human SWI/SNF complex. They had ARID (AT-rich interaction domain) and two high homology region to drosophila Osa. Co-immunoprecipitation study revealed that these C-terminal homology regions were important for the interaction with BRG and BRM, ATP-dependent enzyme componens of SWI/SNF. In cultured cells hOsa stimulated transcription by steroid hormone receptors. ARID lacking mutant did not stimulate the transcription, suggesting the importance of this domain in SWI/SNF function. We established HeLa cell lines which express either wild type or a mutant missing the ARID in Flag-tagged form under the control of tetracycline administration. Putative human SWI/SNF components, Osa, BRG, BAF155, were found in the high molecular weight fractions when the nuclear extracts were separated by glycerol gradient sedimentation. Distribution of BAF170 was different between the extracts from wild type and the mutant expressing cells. There might be some interaction between BAF170 and ARID of Osa-2. Silver staining of the complexes with wild type and the mutant Osa-2 immunopurified from the high molecular weight sedimentation fractions showed quite similar pattern, suggesting the presence of ARID has little effect on the complex formation.
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