Slowly modulating fluctuations as mesoscopic distortions occurring on an actin filament.
An actin filament sliding on myosin molecules exhibits fluctuating or staggered movements as responding to changes in the ATP concentration. We previously observed that fluctuations in the sliding velocity enhanced in a manner being independent of the magnitude of the velocity. The present study focused upon a single actin filament bound to a glass surface through avidin-biotin bonding to examine those fluctuations inherent to the filament in the presence of heavy meromyosin. The auto-correlation analysis revealed that the relaxation time of fluctuations in the filamental displacement obtains its maximum value at about 100microM of the ATP concentration in the ambient, while the magnitude of the fluctuations gradually increased with an increase of the concentration. Furthermore, the measurement of the fluorescence intensity from the markers fixed on the filament demonstrated an enhancement of the negative correlation between the measured peak intensity and the spatial spreading of its intensity over the range of 0-200microM of the ATP concentration, as indicating both development and mitigation of local distortions occurring within the filament.
Hatori
Kuniyuki
K
Department of Bio-System Engineering, Yamagata University, Jyonan, Yonezawa, Japan. khatori@yz.yamagata-u.ac.jp
Matsui
Masahiro
M
Omote
Yoichiro
Y
D008841:Actin Cytoskeleton / Q000737:chemistry* / Q000648:ultrastructure*; D000255:Adenosine Triphosphate / Q000737:chemistry*; D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D009038:Motion; D009218:Myosins / Q000737:chemistry* / Q000648:ultrastructure*; D011487:Protein Conformation
D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D009218:Myosins