Structural basis of the substrate specificity of the alpha-tubulin acetyltransferase
| Project/Area Number |
26440033
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
Yuzawa Satoru 九州大学, 医学研究院, 共同研究員 (40515029)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | 翻訳後修飾 / 微小管 / 酵素 / 基質特異性 / X線結晶構造解析 / 分子認識 / 酵素反応 / 蛋白質 |
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| Outline of Final Research Achievements |
The functions of microtubules are controlled in part by tubulin post-translational modification. αTAT1 is the major α-tubulin acetyltransferase in ciliated organisms and acetylates conserved lysine residue at lysine 40 on α-tubulin proteins by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine. In this study, we determined the crystal structures of αTAT1 bound to its substrate acetyl-CoA or CoA and show the cofactor-mediated stabilization of αTAT1．We also elucidate the recognition of α-tubulin by αTAT1 using wild type and mutant proteins and study on structure of the CoA disulfide bound αTAT1.
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Report
(4 results)
Research Products
(5 results)
