Loading direction regulates the affinity of ADP for kinesin

Sotaro Uemura, Shin'ichi Ishiwata*

*この研究の対応する著者

    研究成果: Article査読

    102 被引用数 (Scopus)

    抄録

    Kinesin is an ATP-driven molecular motor that moves processively along a microtubule. Processivity has been explained as a mechanism that involves alternating single- and double-headed binding of kinesin to microtubules coupled to the ATPase cycle of the motor. The internal load imposed between the two bound heads has been proposed to be a key factor regulating the ATPase cycle in each head. Here we show that external load imposed along the direction of motility on a single kinesin molecule enhances the binding affinity of ADP for kinesin, whereas an external load imposed against the direction of motility decreases it. This coupling between loading direction and enzymatic activity is in accord with the idea that the internal load plays a key role in the unidirectional and cooperative movement of processive motors.

    本文言語English
    ページ(範囲)308-311
    ページ数4
    ジャーナルNature Structural Biology
    10
    4
    DOI
    出版ステータスPublished - 2003 4月 1

    ASJC Scopus subject areas

    • 生化学
    • 構造生物学
    • 遺伝学

    フィンガープリント

    「Loading direction regulates the affinity of ADP for kinesin」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

    引用スタイル