| Project/Area Number |
15590442
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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 |
Immunology
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| Research Institution | TOKYO UNIVERSITY OF SCIENCE |
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Principal Investigator |
MIZUTA Ryushin Tokyo University of Science, Research Institute for Biological Sciences, Assistant professor, 生命科学研究所, 講師 (50297628)
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| Project Period (FY) |
2003 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2004: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2003: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | ubiquitin / proteasome / RAG2 / V(D)J recombination / ubiquitin C-terminal hydrolase / XRCC4 / ユビキチン / プロテオソーム / ユビチキン / AID |
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| Research Abstract |
Ubiquitin/proteasome system plays a major role for target-specific protein degradation and regulation of protein expression level. We previously showed that RAG2 protein, a major machinery of V(D)J recombination, is ubiquitilated and degraded by 26 S proteasome. In this study, we further investigated the involvement of ubiquitin/proteasome system in immune recombination, such as V(D)J recombination and class switch recombination. The results were shown below :
1.Involvement of de-ubiquitin enzyme in V(D)J recombination. XRCC4 protein is involved in double-strand break repair and V(D)J recombination. Using yeast-two hybrid system, we isolated a new XRCC4 associated molecule, named UCH-X4. UCH-X4 turned out to be an ubiquitin C-terminal hydrolase.
2.Generation of UCH-X4 gene-targeting mice. To examine the role of UCH-X4 protein in vivo, we are generating UCH-X4 gene-targeting mice.
3.Some recombination related molecules are degraded by ubiquitin/proteasome system. Using in vivo ubiquitination assay system, we identified several ubiquitilated proteins related to recombination.
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