ATP-dependent fluctuations of single actin filaments in vitro.
Single filaments of actin were observed to fluctuate in the direction perpendicular to their longitudinal axes when they hydrolyzed ATP in the presence of myosin. The transversal fluctuations of actin filaments were identified by reading the transversal displacements of the filaments under a fluorescence microscope. The transversal fluctuations in the absence of ATP decreased their intensity as the number of myosin molecules contacting directly with actin filaments increased. In the presence of ATP, on the other hand, the amplitude of the transversal fluctuations increased in proportion to the ATP concentration up to a certain level, while the sliding velocity of the filaments did not increase significantly over the same range of ATP concentration. The present observation suggests that the chemical energy released from ATP along actin filament binding to myosin molecules is first and primarily converted into kinetic energy of fluctuations in the form of the displacement movements of the filaments in the direction perpendicular to their longitudinal axes.
Hatori
K
K
Department of BioEngineering, Nagaoka University of Technology, Japan.
Honda
H
H
Matsuno
K
K
D000199:Actins / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000737:chemistry*; D000818:Animals; D002417:Cattle; D008856:Microscopy, Fluorescence; D018482:Muscle, Skeletal / Q000737:chemistry; D009218:Myosins / Q000737:chemistry; D051381:Rats
D000199:Actins; D000255:Adenosine Triphosphate; D009218:Myosins