Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle

@article{Yanagida1985SlidingDO,
  title={Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle},
  author={Toshio Yanagida and Toshiaki Arata and Fumio Oosawa},
  journal={Nature},
  year={1985},
  volume={316},
  pages={366-369}
}
Muscle contraction results from a sliding movement of actin filaments induced by myosin crossbridges on hydrolysis of ATP1,2, and many non-muscle cells are thought to move using a similar mechanism3–5. The molecular mechanism of muscle contraction, however, is not completely understood6,7. One of the major problems is the mechanochemical coupling at high velocity under near-zero load8–13. Here, we report measurements of the sliding distance of an actin filament induced by a myosin crossbridge… 

Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibres

The isotonic sliding distance per ATP molecule hydrolysed during the interaction between myosin and actin in skinned muscle fibres is measured and the proportion of simultaneously attached actomyosin complexes and their ATP use is directly estimated.

Rapid regeneration of the actin-myosin power stroke in contracting muscle

The power stroke can be regenerated much faster than expected from the ATPase rate and this contradiction can be resolved if, in the shortening muscle, the free energy of ATP hydrolysis is used in several actin–myosin interactions consisting of elementary power strokes each of 5–10 nm.

Sliding movement of single actin filaments on one-headed myosin filaments

The results show that cooperative interaction between the two heads of myosin is not essential for inducing the sliding movement of actin filaments.

Crossbridge Movements Monitored by Extrinsic Probes

The possibility that the cyclical interaction of myosin and actin during muscle contraction produces muscle shortening against a load is suggested by the observation that the specific actomyosin affinity in a fibre varies over several orders of magnitude, depending on the substrate intermediates that occupy the myOSin ATPase site.

Muscle contraction mechanism based on actin filament rotation.

  • T. Yanagida
  • Biology, Chemistry
    Advances in experimental medicine and biology
  • 2007
Large stepsize of unconventional processive myosin V motor can be explained by its large lever arm within the frame of the lever-arm swinging model.
...

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