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… Expand
Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibres
TLDR
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. Expand
Rapid regeneration of the actin-myosin power stroke in contracting muscle
TLDR
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. Expand
Sliding movement of single actin filaments on one-headed myosin filaments
TLDR
The results show that cooperative interaction between the two heads of myosin is not essential for inducing the sliding movement of actin filaments. Expand
Loose coupling between chemical and mechanical reactions in actomyosin energy transduction.
  • T. Yanagida
  • Chemistry, Medicine
  • Advances in biophysics
  • 1990
TLDR
The resulting sliding distance was greater than 100 nm, which is about 10 times longer than that expected for a single attachment-detachment cycle between an actin monomer and a myosin head, leading to the conclusion that the coupling between the chemical and mechanical reactions is not rigid in a one to one fashion. Expand
Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin.
TLDR
The step size of the myosin cross-bridge in an in vitro motility assay system is estimated by measuring the velocity of slowly moving actin filaments over low densities of heavy meromyosin on a nitrocellulose surface, consistent with a model that predicts that the sliding velocity is determined by the product of vo and the fraction of time when at least one myosIn head is propelling the filament. Expand
Crossbridge Movements Monitored by Extrinsic Probes
An appealing model of the molecular mechanism of muscle contraction proposes that active protein elements of the mechanism move in a cyclical manner in synchrony with the hydrolysis of ATP to produceExpand
Muscle contraction mechanism based on actin filament rotation.
  • T. Yanagida
  • Chemistry, Medicine
  • Advances in experimental medicine and biology
  • 2007
TLDR
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. Expand
Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay.
TLDR
The resulting sliding distance during one ATP hydrolysis cycle near zero load was greater than 100 nm, which is about ten times longer than that expected for a single attachment-detachment cycle between an actin and a myosin head, leading to the conclusion that the coupling between the ATPase and attachment- Detachment cycles is not determined rigidly in a one-to-one fashion. Expand
A self-induced translation model of myosin head motion in contracting muscle I. Force-velocity relation and energy liberation
TLDR
The assumption of co-operativity is eliminated in the present model, following the conclusion by Harada and co-workers that a co-operative interaction between the two heads of myosin is not essential in producing actin filament movement. Expand
Molecular dynamics simulation of a myosin subfragment-1 docking with an actin filament
  • T. Masuda
  • Biology, Computer Science
  • Biosyst.
  • 2013
TLDR
MD simulations successfully reproduced the docking of a myosin S1 with an actin filament, indicating that the docking is stable over time and the validity of the DbD theory may be computationally demonstrated. Expand
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