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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-01

AUTHORS

Kazuo Kitamura, Makio Tokunaga, Atsuko Hikikoshi Iwane, Toshio Yanagida

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. More... »

PAGES

129-134

References to SciGraph publications

  • 1994-03. Single myosin molecule mechanics: piconewton forces and nanometre steps in NATURE
  • 1985-07. Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle in NATURE
  • 1991-07. Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibres in NATURE
  • 1994-12. How molecular motors work in NATURE
  • 1995-04. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution in NATURE
  • 1996-08. Filament compliance and tension transients in muscle in JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
  • 1995. Kernel Smoothing in NONE
  • 1993. Muscle Contraction in NONE
  • 1995-11. Movement and force produced by a single myosin head in NATURE
  • 1993-10. Direct observation of kinesin stepping by optical trapping interferometry in NATURE
  • 1988-07. Force measurements by micromanipulation of a single actin filament by glass needles in NATURE
  • 1992-02. Rapid regeneration of the actin-myosin power stroke in contracting muscle in NATURE
  • 1987-04-01. Sliding movement of single actin filaments on one-headed myosin filaments in NATURE
  • 1971-10. Proposed Mechanism of Force Generation in Striated Muscle in NATURE
  • 1990-09. Atomic structure of the actin: DNase I complex in NATURE
  • 1997-10. Molecular motors: structural adaptations to cellular functions in NATURE
  • 1997-07. Kinesin hydrolyses one ATP per 8-nm step in NATURE
  • 1984-01. Direct observation of motion of single F-actin filaments in the presence of myosin in NATURE
  • 1995-04. What is remembered and why? in NATURE
  • 1991-07. Sub-piconewton force fluctuations of actomyosin in vitro in NATURE
  • 1982-07. F-actin is a helix with a random variable twist in NATURE
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/16403

    DOI

    http://dx.doi.org/10.1038/16403

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1000451350

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9923673


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