F-actin monomer and G-actin did not significantly activate heavy meromyosin Mg2+-ATPase, whereas polymer formation at higher actin or KCl concentrations resulted in substantial activation.
F-actin monomer (F-monomer) is formed upon the addition of neutral salt to G-actin. Since F-monomer has a digestibility similar to that of F-actin and much lower than that of G-actin, it has been proposed that F-monomer has a conformation different from that of G-actin and similar to the conformation of the subunits in F-actin. To examine whether F-monomer will enhance the magnesium-activated myosin adenosine triphosphatase (Mg2+-ATPase) as much as F-actin, the ability of partially polymerized actin populations at equilibrium to activate the Mg2+-ATPase of heavy meromyosin was investigated. Correlations were made between ATPase activities and the polymerization state of actin as determined by measurements of viscosity and digestibility. No significant activation of the heavy meromyosin ATPase was observed under conditions where G-actin or mixtures of G-actin and F-monomer were present. As polymer formation occurred at higher actin concentrations, or with increased KCl concentrations, substantial activation characteristic of F-actin was observed. The data suggest that F-monomer may undergo a further conformational change as it forms nuclei or joins onto polymers. Alternatively, the site of actin which activates the myosin ATPase may involve the crevice between two adjacent actin subunits.
Estes et al. (Tue,) reported a other. Various states of actin (F-monomer, G-actin, F-actin) was evaluated on Activation of heavy meromyosin Mg2+-ATPase. F-actin monomer and G-actin did not significantly activate heavy meromyosin Mg2+-ATPase, whereas polymer formation at higher actin or KCl concentrations resulted in substantial activation.