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

  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},
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.



Direct observation of motion of single F-actin filaments in the presence of myosin

Direct observation by fluorescence microscopy of the movements of single F-actin filaments interacting with soluble myosin fragments energized by Mg2+-ATP is reported.

Structure and Function of the Two Heads of the Myosin Molecule

The myofibrillar ATPase activity reached the saturated level, and with further increase in the concentration of ATP one more mole of ADP was found per mole of myosin, and the amount of ATP required for a constant level of ATP enzyme activity was smaller than that required for the maximum binding ofADP to my ofibrils.

Configurations of myosin heads in the crab striated muscle as studied by X-ray diffraction.

The configurations of myosin projections in striated muscles from the marine crab, Portunus trituberculatus were described in the relaxed and rigor states at the full overlap length of the thin and

Active movement in vitro of bundle of microfilaments isolated from Nitella cell

It is reported here that subcortical fibrils and filaments move actively in an artificial medium containing Mg-ATP and sucrose at neutral pH, when the medium was added to the cytoplasm squeezed out of the cell.

Movement of myosin-coated fluorescent beads on actin cables in vitro

Myosin-coated fluorescent beads are observed to move unidirectionally along organized actin filament arrays in the alga, Nitella, with an average velocity similar to in vivo rates of movement in

Contractile Mechanisms in Muscle

It can be confirmed that a 81 molecule interacts morphologically with actin at two sites, and the major domains A, B and D split into two domains, i.e. into Ai and A2, Hi and B2, and Dl and D2 respectively.