Molecular mechanism of ArfA-mediated ribosome rescue
| Project/Area Number |
16K18684
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied biochemistry
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| Research Institution | Hirosaki University |
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Principal Investigator |
Kurita Daisuke 弘前大学, 農学生命科学部, 准教授 (60552651)
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| Project Period (FY) |
2016-04-01 – 2019-03-31
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| Project Status |
Completed (Fiscal Year 2018)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2018: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | リボソーム / 翻訳 / タンパク合成 / 蛋白質 / 生体分子 / 核酸 |
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| Outline of Final Research Achievements |
Here, using cryo-electron microscopy, we characterize the structure of the Escherichia coli 70S ribosome bound with ArfA, RF2, a short non-stop mRNA and a cognate P-site tRNA. The C-terminal loop of ArfA occupies the mRNA entry channel on the 30S subunit, whereas its N terminus is sandwiched between the decoding centre and the switch loop of RF2, leading to marked conformational changes in both the decoding centre and RF2. Despite the distinct conformation of RF2, its conserved catalytic GGQ motif is precisely positioned next to the CCA-end of the P-site tRNA. These data illustrate a stop-codon surrogate mechanism for ArfA in facilitating the termination of non-stop ribosomal complexes by RF2.
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| Academic Significance and Societal Importance of the Research Achievements |
近年、翻訳停滞解消因子は新しい抗生物質の標的として注目されつつある。一般に、翻訳を阻害する抗生物質はリボソームや翻訳関連因子に作用する。翻訳のメカニズムは生物種を問わず共通しているため、このような抗生物質は広範囲のバクテリアに対して効果を示す。しかし、このような広い抗菌スペクトルを示す薬剤は耐性菌の蔓延リスクを高めるという問題を内包している。翻訳停滞解消因子は結核菌・ピロリ菌・赤痢菌・ペスト菌等の一部の病原菌の生育にとって必須であり、その阻害薬は耐性菌出現リスクの低い次世代の抗生物質として期待される。本研究は、このような薬剤開発の基盤となるものである。
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Report
(4 results)
Research Products
(15 results)
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[Journal Article] RsgA couples the maturation state of the 30S ribosomal decoding center to activation of its GTPase pocket.2017
Author(s)
1.Lopez-Alonso JP, Kaminishi T, Kikuchi T, Hirata Y, Iturrioz I, Dhimole N, Schedlbauer A, Hase Y, Goto S, Kurita D, Muto A, Zhou S, Naoe C, Mills DJ, Gil-Carton D, Takemoto C, Himeno H, Fucini P, Connell SR.
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Journal Title
Nucleic Acids Research
Volume: 40
Issue: 11
Pages: 6945-6959
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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