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Two-headed binding of a processive myosin to F-actin

Author

Listed:
  • Matthew L. Walker

    (Astbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds)

  • Stan A. Burgess

    (Astbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds)

  • James R. Sellers

    (Laboratories of Molecular Cardiology and)

  • Fei Wang

    (Laboratories of Molecular Cardiology and)

  • John A. Hammer

    (National Institutes of Health)

  • John Trinick

    (Astbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds)

  • Peter J. Knight

    (Astbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds)

Abstract

Myosins are motor proteins in cells. They move along actin by changing shape after making stereospecific interactions with the actin subunits1. As these are arranged helically, a succession of steps will follow a helical path. However, if the myosin heads are long enough to span the actin helical repeat (∼36 nm), linear motion is possible. Muscle myosin (myosin II) heads are about 16 nm long2, which is insufficient to span the repeat3. Myosin V, however, has heads of about 31 nm that could span 36 nm (refs 4, 5) and thus allow single two-headed molecules to transport cargo by walking straight5. Here we use electron microscopy to show that while working, myosin V spans the helical repeat. The heads are mostly 13 actin subunits apart, with values of 11 or 15 also found. Typically the structure is polar and one head is curved, the other straighter. Single particle processing reveals the polarity of the underlying actin filament, showing that the curved head is the leading one. The shape of the leading head may correspond to the beginning of the working stroke of the motor. We also observe molecules attached by one head in this conformation.

Suggested Citation

  • Matthew L. Walker & Stan A. Burgess & James R. Sellers & Fei Wang & John A. Hammer & John Trinick & Peter J. Knight, 2000. "Two-headed binding of a processive myosin to F-actin," Nature, Nature, vol. 405(6788), pages 804-807, June.
    • Handle: RePEc:nat:nature:v:405:y:2000:i:6788:d:10.1038_35015592
    DOI: 10.1038/35015592
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    Cited by:

    1. Chou, Y.C., 2019. "Dynamical mechanism of stepping of the molecular motor myosin V along actin filament and simulation in an actual system," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 521(C), pages 399-405.
    2. Tomonobu M Watanabe & Atsuko H Iwane & Hiroto Tanaka & Mitsuo Ikebe & Toshio Yanagida, 2010. "Mechanical Characterization of One-Headed Myosin-V Using Optical Tweezers," PLOS ONE, Public Library of Science, vol. 5(8), pages 1-11, August.

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