| Project/Area Number |
15K12747
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biomolecular chemistry
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| Research Institution | Osaka University |
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Principal Investigator |
Onoda Akira 大阪大学, 工学研究科, 准教授 (60366424)
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| Co-Investigator(Renkei-kenkyūsha) |
HAYASHI Takashi 大阪大学, 大学院工学研究科, 教授 (20222226)
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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 |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 細胞分裂 / タンパク質集合体 / 超分子相互作用 / 活性発現の分子機構 |
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| Outline of Final Research Achievements |
Cell division protein FtsZ assembles as a filamentous structure at midcell leading to the formation of a ring-shaped structure (Z-ring) which constricts to initiate cytoplasmic division. The event involves the conformational change of FtsZ assembly triggered by GTP hydrolysis. To unravel the dynamics and functional aspects of FtsZ assembly, a system in which the assembled structure of engineered FtsZ is perturbed by a supramolecular interaction with external adaptor proteins was developed. FtsZ protein fused with a Strep-tag and a membrane-targeting peptide (Strep-FtsZ-mtp) was found to form a filamentous structure similar to that of the native protein. AFM measurements visualized that the assembly of Strep-FtsZ-mtp was enforced to form a curved structure by the interaction between Strep-tag and streptavidin (Sav). The assembly embedded in a liposome was imaged by fluorescence microscopy.
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