Nucleotide-dependent single- to double-headed binding of kinesin

K. Kawaguchi, S. Ishiwata

    研究成果: Article査読

    104 被引用数 (Scopus)

    抄録

    The motility of kinesin motors is explained by a "hand-over-hand" model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5′-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5′-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model.

    本文言語English
    ページ(範囲)667-669
    ページ数3
    ジャーナルScience
    291
    5504
    DOI
    出版ステータスPublished - 2001 1 26

    ASJC Scopus subject areas

    • General

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