2022 Fiscal Year Final Research Report
TIRF visualization of the polymerization dynamics of bacterial actin cytoskeleton, MreB and A22 driven disruption mechanism
| Project/Area Number |
20K06591
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Review Section |
Basic Section 43040:Biophysics-related
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| Research Institution | Nagaoka University of Technology (2021-2022)
Osaka City University (2020) |
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Principal Investigator |
Fujiwara Ikuko 長岡技術科学大学, 工学研究科, 准教授 (10742075)
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| Project Period (FY) |
2020-04-01 – 2023-03-31
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| Keywords | MreB / A22 / 重合 / タンパク質構造 / アクチン |
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| Outline of Final Research Achievements |
MreB is a bacterial cytoskeleton having a similar shape to actin. An inhibitor A22 is used to study the polymerization of MreB, but it remains unclear which process of MreB polymerization dynamics are inhibited. A22 addition to Spiroplasma disrupted helical swimming, suggesting an interaction between A22 and MreB. Structural analysis of Spiroplasma MreB3 revealed that the differences on ATP hydrolysis site was the cause of slow ATPase. Spiroplasma MreB5 forms a sheet structure in which several filaments are aligned side by side, and MreB5 continues to hydrolyze ATP even after polymerized, suggesting the possibility of renewing the filament structure with a rapid turnover.
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| Free Research Field |
生物物理
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| Academic Significance and Societal Importance of the Research Achievements |
多くの細菌に存在し、細胞の形態維持に必須であるMreBのタンパク質としての機能の解明は難しい。この理由として、菌体におけるMreBの影響を調べる研究が、重合阻害剤A22またはMreB欠損株から得られたものしかなく、MreBの重合・脱重合という、菌の形を保つために必須の動的ダイナミクスの相関が未解明であることが挙げられる。これら病原菌に対し、A22による阻害メカニズムの理解は、分子レベルで病原性細菌の運動メカニズムの理解につなげられる点で意義が大きく、A22を基にして、創薬や病原体診断・検査、治療、及び予防法の開発に応用できる可能性を含む。以上から基礎学術をはじめ、多分野にて役立つ研究である。
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