Analysis of budding yeast E3 ubiquitin ligases that regulate the degradation of short life protein
| Project/Area Number |
15K14474
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Functional biochemistry
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| Research Institution | Nagoya University |
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Principal Investigator |
Kamura Takumi 名古屋大学, 理学研究科, 教授 (40333455)
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| Co-Investigator(Kenkyū-buntansha) |
中務 邦雄 名古屋大学, 理学研究科, 講師 (90547522)
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | タンパク質分解 |
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| Outline of Final Research Achievements |
In this study, we searched for E3s which control the stability of the substrates to clarify various phenomenon regulated by the ubiquitin proteasome system. We chose several functionally important short life proteins using a database for protein half-life of the budding yeast. We identified E3s which controlled the degradation of these proteisn using E3 deletion strains. As a result, we found p70, p75, p75, p65 and p150 and p340 as E3s which controlled the degradation of Nup1, Tma17, Hcm1, Cdc1 and Spo12. In addition, we clarified the physiological significance of the Spo12 degradation mediated by p340. Our findings shed the light on the new function of ubiquitin proteasome system.
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Report
(3 results)
Research Products
(20 results)
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[Journal Article] The ubiquitin ligase SCFUcc1 acts as a metabolic switch for the glyoxylate cycle.2015
Author(s)
Nakatsukasa, K., Nishimura, T., Byrne, D., Okamoto, M., Takahashi-Nakaguchi, A., Chibana, H., Okumura, F., Kamura, T.
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Journal Title
Molecular Cell
Volume: 59
Issue: 1
Pages: 22-34
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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