| Project/Area Number |
13043006
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| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas
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| Allocation Type | Single-year Grants |
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| Review Section |
Biological Sciences
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| Research Institution | The University of Tokyo |
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Principal Investigator |
TOH-E Akio The University of Tokyo, Department of Biological Sciences, Professor, 大学院理学研究科, 教授 (90029249)
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| Co-Investigator(Kenkyū-buntansha) |
菊池 淑子 東京大学, 大学院・理学系研究科, 助教授 (00138124)
吉田 稔 東京大学, 大学院・農学生命科学研究科, 助教授 (80191617)
安田 秀世 東京薬科大学, 生命科学部, 教授 (40111554)
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| Project Period (FY) |
2001 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥118,800,000 (Direct Cost: ¥118,800,000)
Fiscal Year 2005: ¥22,700,000 (Direct Cost: ¥22,700,000)
Fiscal Year 2004: ¥22,100,000 (Direct Cost: ¥22,100,000)
Fiscal Year 2003: ¥24,400,000 (Direct Cost: ¥24,400,000)
Fiscal Year 2002: ¥25,500,000 (Direct Cost: ¥25,500,000)
Fiscal Year 2001: ¥24,100,000 (Direct Cost: ¥24,100,000)
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| Keywords | 26S proteasome / 19S reguratory comoplex / base / baker's yeast / lid / RPN7 / RPN6 / RPN5 / ユビキチン・プロテアソーム系 / サブユニット集合 / RPN8 / 局在 / 出芽酵母 / ユビキチン / M期後期開始 / RPN9 / 蛋白質分解 / G2 / Mアレスト / プロテアソーム / 阻害剤 / M期終了 / Cdc14 / 核小体 / MEN / Tem1 / SPB / スピンドルチェックポイント / Cdc14フォスファスーゼ |
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| Research Abstract |
It is widely accepted that the ubiquitin-proteasome system plays a pivotal role in degradation of short-lived proteins, many of them are regulatory proteins, in an energy dependent manner. The 26S proteasome is responsible to the final step of proteolysis in this system. The 26S proteasome is a large protein complex consisting of 20S proteasome containing active sites and 19S regulatory factor called as 19S RP. The basic subunit composition has been elucidated. By exploiting this information, we started uncovering how and where these subunits assemble together. We focused on the 19S RP of Saccharomyces cerevisiae. The 19S RP consists of two sub-complexes, the lid and the base. We isolated temperature-sensitive mutants of the genes encoding subunits of the lid. Biochemical characterization revealed that hierarchy of the assembly of the lid, and the lid and the base are constructed independently of each other. We also examined localization of each sub-complex in various mutants and found that the base and the lid can separately be localized in the nucleus. The 19S RP too is localized in the nucleus and assembles with the 20S proteasome to the 26S proteasome.
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