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A single myosin head moves along an actin filament with regular steps of 5.3 nanometres

Author

Listed:
  • Kazuo Kitamura

    (Yanagida BioMotron Project, ERATO, JST
    Osaka University
    Osaka University Medical School)

  • Makio Tokunaga

    (Yanagida BioMotron Project, ERATO, JST
    Structural Biology Center, National Institute of Genetics)

  • Atsuko Hikikoshi Iwane

    (Osaka University
    Osaka University Medical School)

  • Toshio Yanagida

    (Yanagida BioMotron Project, ERATO, JST
    Osaka University
    Osaka University Medical School
    Single Molecule Processes Project, ICORP, JST)

Abstract

Actomyosin, a complex of actin filaments and myosin motor proteins, is responsible for force generation during muscle contraction. To resolve the individual mechanical events of force generation by actomyosin, we have developed a new instrument with which we can capture and directly manipulate individual myosin subfragment-1 molecules using a scanning probe. Single subfragment-1 molecules can be visualized by using a fluorescent label. The data that we obtain using this technique are consistent with myosin moving along an actin filament with single mechanical steps of approximately 5.3 nanometres; groups of two to five rapid steps in succession often produce displacements of 11 to 30 nanometres. This multiple stepping is produced by a single myosin head during just one biochemical cycle of ATP hydrolysis.

Suggested Citation

  • Kazuo Kitamura & Makio Tokunaga & Atsuko Hikikoshi Iwane & Toshio Yanagida, 1999. "A single myosin head moves along an actin filament with regular steps of 5.3 nanometres," Nature, Nature, vol. 397(6715), pages 129-134, January.
  • Handle: RePEc:nat:nature:v:397:y:1999:i:6715:d:10.1038_16403
    DOI: 10.1038/16403
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    Cited by:

    1. Qing-Miao Nie & Akio Togashi & Takeshi N Sasaki & Mitsunori Takano & Masaki Sasai & Tomoki P Terada, 2014. "Coupling of Lever Arm Swing and Biased Brownian Motion in Actomyosin," PLOS Computational Biology, Public Library of Science, vol. 10(4), pages 1-13, April.
    2. Lorenzo Marcucci & Takumi Washio & Toshio Yanagida, 2016. "Including Thermal Fluctuations in Actomyosin Stable States Increases the Predicted Force per Motor and Macroscopic Efficiency in Muscle Modelling," PLOS Computational Biology, Public Library of Science, vol. 12(9), pages 1-20, September.

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