Kinesin-microtubule binding depends on both nucleotide state and loading direction

Sotaro Uemura, Kenji Kawaguchi, Junichiro Yajima, Masaki Edamatsu, Yoko Yano Toyoshima, Shin'ichi Ishiwata*


    研究成果: Article査読

    105 被引用数 (Scopus)


    Kinesin is a motor protein that transports organelles along a microtubule toward its plus end by using the energy of ATP hydrolysis. To clarify the nucleotide-dependent binding mode, we measured the unbinding force for one-headed kinesin heterodimers in addition to conventional two-headed kinesin homodimers under several nucleotide states. We found that both a weak and a strong binding state exist in each head of kinesin corresponding to a small and a large unbinding force, respectively; that is, weak for the ADP state and strong for the nucleotide-free and adenosine 5′-[β,γ-imido]triphosphate states. Model analysis showed that (i) the two binding modes in each head could be explained by a difference in the binding energy and (ii) the directional instability of binding, i.e., dependence of unbinding force on loading direction, could be explained by a difference in the characteristic distance for the kinesin-microtubule interaction during plus- and minus-end-directed loading. Both these factors must play an important role in the molecular mechanism of kinesin motility.

    ジャーナルProceedings of the National Academy of Sciences of the United States of America
    出版ステータスPublished - 2002 4月 30

    ASJC Scopus subject areas

    • 遺伝学
    • 一般


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