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Direct observation of the mechanochemical coupling in myosin Va during processive movement

Author

Listed:
  • Takeshi Sakamoto

    (Laboratory of Molecular Physiology, National Heart, Lung and Blood Institute, Bethesda, Maryland 20892, USA)

  • Martin R. Webb

    (MRC National Institute for Medical Research, Mill Hill, London NW7 1AA, UK)

  • Eva Forgacs

    (Eastern Virginia Medical School, Norfolk, Virginia 23507, USA)

  • Howard D. White

    (Eastern Virginia Medical School, Norfolk, Virginia 23507, USA)

  • James R. Sellers

    (Laboratory of Molecular Physiology, National Heart, Lung and Blood Institute, Bethesda, Maryland 20892, USA)

Abstract

Myosin V motors: in step with ATP Myosin Va is a two-headed molecular motor which transports cargo inside cells by moving along actin filaments. The trailing head detaches and swings 72 nm forward to bind to a new leading position. During the processive movement at least one of the heads remain bound to actin. In this report Sellers and colleagues visualized the movement of a fluorescently labelled myosin Va molecule while simultaneously observing the binding and dissociation of a fluorescent ATP analogue. Each head swing is tightly coupled to the binding and dissociation of the nucleotide and the lead head retains nucleotide, presumably the diphosphate form, as long as the trail head is attached indicating gating between the two heads. This is the first direct demonstration of nucleotide binding to and movement of myosin V motors during stepping.

Suggested Citation

  • Takeshi Sakamoto & Martin R. Webb & Eva Forgacs & Howard D. White & James R. Sellers, 2008. "Direct observation of the mechanochemical coupling in myosin Va during processive movement," Nature, Nature, vol. 455(7209), pages 128-132, September.
    • Handle: RePEc:nat:nature:v:455:y:2008:i:7209:d:10.1038_nature07188
    DOI: 10.1038/nature07188
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