Structural Basis of tRNA modification at position 37
Project/Area Number |
20770077
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Structural biochemistry
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Research Institution | The University of Tokyo |
Principal Investigator |
ITO Takuhiro The University of Tokyo, 大学院・理学系研究科, 助教 (70401164)
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Project Period (FY) |
2008 – 2009
|
Project Status |
Completed (Fiscal Year 2009)
|
Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2009: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2008: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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Keywords | タンパク質 / 核酸 / tRNA / 修飾塩基 / X線結晶構造解析 / 立体構造 |
Research Abstract |
The crystal structure of the TRM5・tRNA・AdoMet complex was determined. TRM5 is the enzyme that transfers a methyl moiety from a methyl-donor AdoMet to the N1 position of G37 in tRNA. TRM5 has two structural domains, D1 and D2-D3, to recognize a substrate tRNA. We clarified that D2-D3 transfers methyl moiety to G37, only when D1 recognizes the establishment of the L-shaped tRNA structure. Therefore, TRM5 may function as a checkpoint for the quality of the tRNA maturation.
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Report
(3 results)
Research Products
(11 results)
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[Journal Article] Crystal Structure of Archaeal tRNA (m1G37) methyltransferase aTRM52008
Author(s)
Goto-Ito, S., Ito, T., Ishii, R., Muto, Y., Bessho, Y., Yokoyama, S.
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Journal Title
PROTEINS: Structure, Function, and Bioinformatics 72
Pages: 1274-1289
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