Investigation of a cytosolic sulfur transfer pathway for tRNA thio-modification and biosynthesis of sulfur-containing molecules
| Project/Area Number |
21570150
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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 | Osaka Medical College |
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Principal Investigator |
NAKAI Yumi 大阪医科大学, 医学部, 講師 (80268193)
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| Project Period (FY) |
2009 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2011: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2010: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2009: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | tRNA硫黄修飾 / 酵母 / ミトコンドリア / サイトゾル / 鉄硫黄クラスター / システインデスルフラーゼ / tRNA修飾 / ロダネーゼ / ユビキチン様タンパク質 / 硫黄付加 / 含硫小分子 / チオカルボキシル基 / 硫黄運搬 |
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| Research Abstract |
We found that ubiquitin-like protein Urm1 and ubiquitin-activating enzyme-like protein Uba4 were strictly required for the s2 modification. The carboxyl-terminal glycine residue of Urm1 was critical for the s2 modification, indicating direct involvement of the unique ubiquitin-related system in this process. We also demonstrated that the s2 and mcm5 modifications in cytosolic tRNAs influence each other's efficiency. Taken together, our data indicate that the s2 modification of cytosolic tRNAs is a more complex process that requires additional unidentified components.
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Report
(4 results)
Research Products
(14 results)
