Stochastic properties of actomyosin motor.
The epoch-making techniques for manipulating a single myosin molecule have recently been developed, and the unitary mechanical reactions of a single actomyosin, muscle motor molecule, are directly measured. The data show that the unitary mechanical step during sliding along an actin filament of approximately 5.5 nm, but groups of two to five rapid steps in succession produce displacements of approximately 11-30 nm. The instances of multiple stepping are produced by single myosin heads during one biochemical cycle of ATP hydrolysis. Thus, the coupling between ATP hydrolysis cycle and mechanical step is variable, i.e. loose-coupling. Such a unique operation of actomyosin molecules is different from that of man-made machines, and most likely explains the flexible and effective mechanisms of molecular machines in the biosystems.
Kitamura
Kazuo
K
Single Molecule Processes Project, ICORP, JST, 2-4-14 Senba-higashi, Mino, Osaka 562-0035, Japan. k.kitamura@ucl.ac.uk
Yanagida
Toshio
T
D000199:Actins / Q000502:physiology; D000205:Actomyosin / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D006868:Hydrolysis; D066298:In Vitro Techniques; D008856:Microscopy, Fluorescence / Q000295:instrumentation; D020527:Microscopy, Scanning Probe / Q000295:instrumentation; D008954:Models, Biological; D020409:Molecular Motor Proteins / Q000502:physiology*; D009218:Myosins / Q000502:physiology; D013269:Stochastic Processes
D000199:Actins; D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D000205:Actomyosin; D009218:Myosins