Cooperativity between the two heads of rabbit skeletal muscle heavy meromyosin in binding to actin.
An extensive series of experiments in this laboratory has shown that the binding of actin to rabbit skeletal muscle myosin subfragment-1 (a single-headed subfragment) can be described by a two-step model, with formation of a weakly bound complex, the A-state, followed by an isomerization to a more tightly bound complex, the R-state. In this paper, we report on additional experiments comparing the subfragment-1 with heavy meromyosin (a two-headed subfragment). Using a modeling approach, we have quantitated the two-step binding for each of the two heads. This indicates that the binding is cooperative and leads to a more complex view of the acto-myosin interaction than has previously been acknowledged. Implications for the dynamic behavior of the two heads during muscle contraction are discussed.
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, United Kingdom. pbc1@le.ac.uk
P B
PB
Conibear
M A
MA
Geeves
D000199:Actins / Q000737:chemistry* / Q000378:metabolism*; D000205:Actomyosin / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D018482:Muscle, Skeletal / Q000378:metabolism; D015879:Myosin Subfragments / Q000737:chemistry* / Q000378:metabolism*; D009218:Myosins / Q000737:chemistry / Q000378:metabolism; D010590:Phalloidine / Q000494:pharmacology; D011817:Rabbits; D013997:Time Factors
D000199:Actins; D015879:Myosin Subfragments; D010590:Phalloidine; D000205:Actomyosin; D009218:Myosins