Elucidation of the structural basis for the interaction of the ribosomal stalk protein with aminoacyl-tRNA synthetase
Project/Area Number |
15K06964
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Structural biochemistry
|
Research Institution | Niigata University |
Principal Investigator |
Kosuke Ito 新潟大学, 自然科学系, 助教 (20502397)
|
Co-Investigator(Kenkyū-buntansha) |
三好 智博 松本歯科大学, 歯学部, 講師 (60534550)
|
Co-Investigator(Renkei-kenkyūsha) |
UCHIUMI Toshio 新潟大学, 自然科学系, 教授 (50143764)
|
Project Period (FY) |
2015-04-01 – 2018-03-31
|
Project Status |
Completed (Fiscal Year 2017)
|
Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
|
Keywords | リボソーム / 触手様タンパク質 / アミノアシルtRNA合成酵素 / 翻訳 / X線結晶構造解析 |
Outline of Final Research Achievements |
The ribosomal stalk protein moves in a broad range on the ribosome. The ribosomal stalk protein directly interacts with and recruits the translation factors to the ribosome. On the other hand, recently it was found that the ribosomal stalk protein also binds to aminoacyl-tRNA synthetase and contributes to the efficient supply of aminoacyl-tRNA to the translation elongation factor. In our present research, we first conducted the analysis of the interaction between the ribosomal stalk protein and aminoacyl-tRNA synthetase. The results suggested that the N-terminal region of the C-terminal domain of the stalk protein is important for the binding. In addition, we obtained the microcrystals of the stalk protein-aminoacyl-tRNA complex.
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Report
(4 results)
Research Products
(6 results)