Mechanochemical coupling of two substeps in a single myosin V motor

Sotaro Uemura, Hideo Higuchi, Adrian O. Olivares, Enrique M. De La Cruz, Shin'ichi Ishiwata

    Research output: Contribution to journalArticle

    144 Citations (Scopus)

    Abstract

    Myosin V is a double-headed processive molecular motor that moves along an actin filament by taking 36-nm steps. Using optical trapping nanometry with high spatiotemporal resolution, we discovered that there are two possible pathways for the 36-nm steps, one with 12- and 24-nm substeps, in this order, and the other without substeps. Based on the analyses of effects of ATP, ADP and 2,3-butanedione 2-monoxime (a reagent shown here to slow ADP release from actomyosin V) on the dwell time and the occurrence frequency of the main and the intermediate states, we propose that the 12-nm substep occurs after ATP binding to the bound trailing head and the 24-nm substep results from a mechanical step following the isomerization of an actomyosin-ADP state on the bound leading head. When the isomerization precedes the 12-nm substep, the 36-nm step occurs without substeps.

    Original languageEnglish
    Pages (from-to)877-883
    Number of pages7
    JournalNature Structural and Molecular Biology
    Volume11
    Issue number9
    DOIs
    Publication statusPublished - 2004 Sep

    ASJC Scopus subject areas

    • Structural Biology
    • Molecular Biology

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  • Cite this

    Uemura, S., Higuchi, H., Olivares, A. O., De La Cruz, E. M., & Ishiwata, S. (2004). Mechanochemical coupling of two substeps in a single myosin V motor. Nature Structural and Molecular Biology, 11(9), 877-883. https://doi.org/10.1038/nsmb806