Molecular mechanism of enzyme complexes catalyzing two-step reaction for Cys-tRNA synthesis
Project/Area Number |
15H04334
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | Hokkaido University |
Principal Investigator |
Tanaka Isao 北海道大学, 先端生命科学研究院, 名誉教授 (70093052)
|
Co-Investigator(Kenkyū-buntansha) |
姚 閔 北海道大学, 先端生命科学研究院, 教授 (40311518)
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Project Period (FY) |
2015-04-01 – 2018-03-31
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Project Status |
Completed (Fiscal Year 2017)
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Budget Amount *help |
¥16,380,000 (Direct Cost: ¥12,600,000、Indirect Cost: ¥3,780,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2016: ¥6,240,000 (Direct Cost: ¥4,800,000、Indirect Cost: ¥1,440,000)
Fiscal Year 2015: ¥8,580,000 (Direct Cost: ¥6,600,000、Indirect Cost: ¥1,980,000)
|
Keywords | X線結晶構造解析 / tRNA修飾 / アミノアシル合成酵素 / X線結晶構造解析 / rRNA修飾 / X線結晶解析 / アミノアシル化反応 / tRNA |
Outline of Final Research Achievements |
For synthesizing a protein from DNA base sequence, it is necessary to correctly bind the amino acid to the transfer RNA (aminoacylation reaction), and usually the enzyme called aminoacyl tRNA synthetase (aaRS) plays its role. However, in methanogenic archaebacteria, an enzyme complex called transsulfursome (SepRS: SepCysE: SepCysS) does. In this study, the reaction mechanism of this system was clarified using X-ray crystal structure analysis method, X-ray small angle scattering method, electron microscope observation and other biochemical methods. Transsulfursome is thought to be the ancestral aminoacylation system. Therefore, it is expected that this research will go a step further to elucidate the mystery related to the birth of the genetic code in the future.
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Report
(4 results)
Research Products
(16 results)
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[Journal Article] Structural basis for tRNA-dependent cysteine biosynthesis2017
Author(s)
Chen Meirong、Kato Koji、Kubo Yume、Tanaka Yoshikazu、Liu Yuchen、Long Feng、Whitman William B.、Lill Pascal、Gatsogiannis Christos、Raunser Stefan、Shimizu Nobutaka、Shinoda Akira、Nakamura Akiyoshi、Tanaka Isao、Yao Min
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Journal Title
Nature Commun.
Volume: 8
Issue: 1
Pages: 1521-1521
DOI
NAID
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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