Mutual sensitization of ATP and GTP in driving F-actin on the surface-fixed H-meromyosin.
Using an in vitro motility assay on acto-H-meromyosin, we studied the sliding velocity of an actin filament driven by two kinds of H-meromyosin heads: H-meromyosin head with ATP bound (fast motor) and with GTP bound (slow motor). We found a significant increase in the sliding velocity owing to the coexistence of the fast motor and the slow motor. This phenomenon may give an important suggestion with regard to the integration over multiple interactions of H-meromyosin heads along the actin filament.
Oda
T
T
Department of Physics, Faculty of Science, Nagoya University, Japan.
Shikata
Y
Y
Mihashi
K
K
D000199:Actins / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D016244:Guanosine 5'-O-(3-Thiotriphosphate) / Q000494:pharmacology; D006153:Guanosine Diphosphate / Q000494:pharmacology; D006160:Guanosine Triphosphate / Q000378:metabolism*; D007700:Kinetics; D018482:Muscle, Skeletal / Q000378:metabolism; D015879:Myosin Subfragments / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits
D000199:Actins; D015879:Myosin Subfragments; D006153:Guanosine Diphosphate; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate