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Mechanical stability of microtubules investigated under unidirectional strain using combined fluorescence microscopy and high-speed atomic force microscopy

Research Project

Project/Area Number 20K03889
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeMulti-year Fund
Section一般
Review Section Basic Section 13040:Biophysics, chemical physics and soft matter physics-related
Research InstitutionCenter for Novel Science Initatives, National Institutes of Natural Sciences

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)

Project Period (FY) 2020-04-01 – 2023-03-31
Project Status Completed (Fiscal Year 2022)
Budget Amount *help
¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
Fiscal Year 2022: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2021: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2020: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
KeywordsMicrotubules / HS-AFM / TIRFM / deformation / microtubules / Mechanical Properties / high-speed AFM / mechanical properties / correlated imaging
Outline of Research at the Start

Microtubules (MTs) are stiff protein tubes found in eukaryotic cells and require a certain stability to function. In this project, the reaction of MTs to external strain will be investigated. The experiments will utilize high-speed atomic force microscopy combined with fluorescence microscopy.

Outline of Final Research Achievements

An elastic substrate stretching device to be used with a tip-scan high-speed atomic force microscope (HS-AFM) was develeloped and used to load microtubules fixed by sparsely distributed kinesin. Due to the elastic substrate experiencing simultaneous tension and compression caused by Poisson's effect, buckling of microtubules could be recorded in a controlled manner. Imaging was perfomed with a resolution of several nanometers, surpassing the resolution of conventional fluorescence microscopy. Further, stretching of microtubules could also be observed, which lead to the microtubules fracturing and depolymerizing.
Using a different approach, microtubules were self-assembled into rings by DNA-modification on kinesin substrates. These rings turned out to have a complex 3D structure that was elucidated by combined HS-AFM and TIRFM.

Academic Significance and Societal Importance of the Research Achievements

A system that allows to intrinsically apply stress to any number of samples was developed and can be used study membrane mechanics or mechanical properties of soft material on a large scale. Furthermore, ring-shaped microtubule swarms could be utilized as motors for nanomachines.

Report

(4 results)
  • 2022 Annual Research Report   Final Research Report ( PDF )
  • 2021 Research-status Report
  • 2020 Research-status Report
  • Research Products

    (8 results)

All 2023 2022 2021 2020

All Journal Article (2 results) (of which Int'l Joint Research: 1 results,  Peer Reviewed: 2 results,  Open Access: 1 results) Presentation (6 results) (of which Int'l Joint Research: 1 results,  Invited: 2 results)

  • [Journal Article] 3D Structure of Ring-shaped Microtubule Swarms Revealed by High-speed Atomic Force Microscopy2023

    • Author(s)
      Rashid Mst. Rubaya、Ganser Christian、Akter Mousumi、Nasrin Syeda Rubaiya、Kabir Arif Md. Rashedul、Sada Kazuki、Uchihashi Takayuki、Kakugo Akira
    • Journal Title

      Chemistry Letters

      Volume: 52 Issue: 2 Pages: 100-104

    • DOI

      10.1246/cl.220491

    • Related Report
      2022 Annual Research Report
    • Peer Reviewed / Open Access / Int'l Joint Research
  • [Journal Article] Tip-scan high-speed atomic force microscopy with a uniaxial substrate stretching device for studying dynamics of biomolecules under mechanical stress2022

    • Author(s)
      Chan Feng-Yueh、Kurosaki Ryo、Ganser Christian、Takeda Tetsuya、Uchihashi Takayuki
    • Journal Title

      Review of Scientific Instruments

      Volume: 93 Issue: 11 Pages: 113703-113703

    • DOI

      10.1063/5.0111017

    • Related Report
      2022 Annual Research Report
    • Peer Reviewed
  • [Presentation] Studying the motor protein kinesin with high-speed atomic force microscopy2021

    • Author(s)
      Christian Ganser
    • Organizer
      International Symposium on Nanoscale Research
    • Related Report
      2021 Research-status Report
    • Invited
  • [Presentation] Kinesin motility inhibition studied by HS-AFM2021

    • Author(s)
      Christian Ganser
    • Organizer
      4th ExCELLS Young Researchers Retreat
    • Related Report
      2021 Research-status Report
  • [Presentation] The influence of microtubule deformation on kinesin motility studied with HS-AFM2021

    • Author(s)
      Christian Ganser
    • Organizer
      4th ExCELLS Symposium
    • Related Report
      2021 Research-status Report
  • [Presentation] High-speed atomic force microscopy based force mapping and multiscale observation in combination with fluorescence microscopy2020

    • Author(s)
      Christian Ganser
    • Organizer
      3rd ExCELLS retreat for young researchers
    • Related Report
      2020 Research-status Report
  • [Presentation] High-speed atomic force microscopy as a versatile tool to study dynamical and mechanical properties of proteins2020

    • Author(s)
      Christian Ganser, Kimitoshi Takeda, Ryota Iino, Koichi Kato, Takayuki Uchihashi
    • Organizer
      The 58th Annual Meeting of the Biophysical Society of Japan
    • Related Report
      2020 Research-status Report
    • Int'l Joint Research / Invited
  • [Presentation] Multimodal high-speed atomic force microscopy to investigate nano-scalemechanical properties and dynamics on the protein and cell level2020

    • Author(s)
      Shigetaka Nishiguchi, Christian Ganser
    • Organizer
      3rd ExCELLS Symposium
    • Related Report
      2020 Research-status Report

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Published: 2020-04-28   Modified: 2024-01-30  

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