Temperature dependence of the flexural rigidity of single microtubules

Kenji Kawaguchi, Shin'ichi Ishiwata, Toshihide Yamashita

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    22 Citations (Scopus)

    Abstract

    Although the flexural rigidity of a microtubule has previously been estimated by various methods, its temperature dependence has never been systematically examined. Here, we measured the flexural rigidity of a single taxol-stabilized microtubule from thermal fluctuation of the free end of a microtubule, the other end of which was fixed, at different temperatures; the results showed that the flexural rigidity is 2.54 × 10-24 N m2 independent of temperature in the range of 20-35 °C. Next, we applied temperature pulse microscopy (TPM) [K. Kawaguchi, S. Ishiwata, Thermal activation of single kinesin molecules with temperature pulse microscopy. Cell Motil. Cytoskeleton 49 (2001) 41-47; H. Kato, T. Nishizaka, T. Iga, K. Kinosita Jr., S. Ishiwata, Imaging of thermal activation of actomyosin motors. Proc. Natl. Acad. Sci. USA 96 (1999) 9602-9606], which created the temperature gradient (1-2 °C/μm) along a microtubule gliding on kinesins in the presence of ATP. As a result, the gliding microtubule was buckled between two interacting kinesin molecules, when the microtubule had been propelled faster by the rear kinesin (higher temperature) and slower by the front one (lower temperature). By estimating the critical force to induce buckling of a microtubule, the flexural rigidity of a microtubule was estimated to be (2.7-7.8) × 10-24 N m2, which was in good agreement with the value determined above. We discuss the buckling process based on the temperature dependence of the force-velocity relationship of kinesin motility.

    Original languageEnglish
    Pages (from-to)637-642
    Number of pages6
    JournalBiochemical and Biophysical Research Communications
    Volume366
    Issue number3
    DOIs
    Publication statusPublished - 2008 Feb 15

    Keywords

    • Flexural rigidity
    • Kinesin
    • Microtubule
    • Motor protein
    • Temperature pulse microscopy (TPM)

    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Molecular Biology

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