Elucidation of dynamic-molecular recognition mechanism by the dimeric RNA maturation enzymes
| Project/Area Number |
15K06975
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
Structural biochemistry
|
|---|
| Research Institution | Ehime University |
|---|
Principal Investigator |
Hirata Akira 愛媛大学, 理工学研究科(工学系), 講師 (60527381)
|
|---|
| Project Period (FY) |
2015-04-01 – 2018-03-31
|
| Project Status |
Completed (Fiscal Year 2017)
|
| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2017: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Fiscal Year 2016: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
|
|---|
| Keywords | tRNA maturation / tRNA modification / recognition mechanism / X-ray structure / SAXS analysis / tRNA methyltransferase / RNA splicing / アーキア / 酵母 / X線結晶構造解析 / tRNA成熟 / 基質認識 / tRNAスプライシング / X線溶液散乱 / RNA成熟 / 動的分子認識機構 |
|---|
| Outline of Final Research Achievements |
The X-ray structure of archaeal aTrm11, which is homologous to the catalytic unit of Trm11 in eukaryotic tRNA (m2G10) methyltransferase Trm11-Trm112, is determined, and the structure-guided biochemical analysis provides mechanistic insight into site specificity of archaeal Trm11 and furher proposes a molecular ruler mechanism by which the Trm11 defines the distance and angle from the end of 3'-CCA in substrate tRNA to methylation site. The structural and functional analyses of RNA-splicing endonuclease (EndA) from hyperthermophilic archaeon Methanopyrus kandleri have demonstrated that the MKA EndA consists of heterodimer （αβ)2 and shows a constrain substrate specificity.
|
Report
(4 results)
Research Products
(16 results)
