Novel function of tyrosyl-and tryptophanyl-tRNA synthetases
| Project/Area Number |
21570129
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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 | The University of Tokyo |
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Principal Investigator |
WAKASUGI Keisuke 東京大学, 大学院・総合文化研究科, 准教授 (20322167)
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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 |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2011: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2010: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2009: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | 蛋白質 / 酵素 / 新規機能 / 血管新生 / 制御機構 |
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| Research Abstract |
Human tryptophanyl-tRNA synthetase(TrpRS) catalyzes the aminoacylation of tRNATrp. Human TrpRS exists in two forms : a major form that is the full-length protein and a truncated form(mini TrpRS). Human mini, but not full-length, TrpRS has angiostatic activity. In the present study, I searched for conformational differences between the two proteins and showed that the molecular environment around Cys62 is significantly different between the two proteins. Previously, I demonstrated that binding of Zn2+or heme to human TrpRS stimulates its aminoacylation activity. In the present study, bovine and mouse TrpRSs were found to be constitutively active regardless of the presence of Zn2+or heme. Mutagenesis experiments demonstrated that the human H130R mutant is constitutively active and that the bovine R135H, E438A double mutant binds with Zn2+or heme to enhance its aminoacylation activity as does human wild-type TrpRS.
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Report
(4 results)
Research Products
(16 results)
