| Project/Area Number |
19K23737
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Multi-year Fund |
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| Review Section |
0701:Biology at molecular to cellular levels, and related fields
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| Research Institution | Center for Novel Science Initatives, National Institutes of Natural Sciences |
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Principal Investigator |
Ganser Christian 大学共同利用機関法人自然科学研究機構(新分野創成センター、アストロバイオロジーセンター、生命創成探究, 生命創成探究センター, 特任助教 (50846095)
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| Project Period (FY) |
2019-08-30 – 2021-03-31
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| Project Status |
Completed (Fiscal Year 2020)
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| Budget Amount *help |
¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
Fiscal Year 2020: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2019: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | HS-AFM / kinesin / microtubules / TIRFM / high-speed AFM / AFM force curves / Kinesin / Motor proteins / Microtubules / Motor Protein / Microtubule |
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| Outline of Research at the Start |
Microtubules are protein tubes that act as highways for so-called motor proteins. If motor proteins are hindered, diseases such as Alzheimer's can arise. In this project, atomic force microscopy and fluorensence microscopy are used to study how defects influence the motor protein motility.
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| Outline of Final Research Achievements |
In this project, an existing system then combined high-speed atomic force microscopy (HS-AFM) with total internal reflection fluorescence microscopy (TIRFM) as well as a conventional HS-AFM system were used to study the motility of kinesin on microtubules. Kinesin could be observed at different concentrations of adenosine triphosphate (ATP) with conventional HS-AFM and showed a behavior expected from literature. This confirmed that HS-AFM is suitable to image kinesin motility with minimum invasiveness. Further, the combined HS-AFM/TIRFM system was improved significantly and allowed to observe movement of kinesin with HS-AFM and TIRFM simultaneously.
It was found that small defects can actually be overcome by kinesin. However, the detailed investigation of how defects in the microtubule lattice will impact kinesin motility is still ongoing. This proces requires extensive measurements with the combined system at different ATP concentrations and with various defect sizes.
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| Academic Significance and Societal Importance of the Research Achievements |
HS-AFMとTIRFMを組み合わせてモータータンパク質を研究する新たなアプローチを導入しました。
このアプローチは、HS-AFMの空間分解能とTIRFMの広域観測能および時間分解能を組み合わせたマルチスケール観測によるものです。
これは、モータータンパク質の研究に大きなインパクトを与え、モータータンパク質の理解を深めるのに役立つものとなります。
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