Rate of binding of tropomyosin to actin filaments.
The decrease of the rate of actin polymerization by tropomyosin molecules which bind near the ends of actin filaments was analyzed in terms of the rate of binding of tropomyosin to actin filaments. Monomeric actin was polymerized onto actin filaments in the presence of various concentrations of tropomyosin. At high concentrations of monomeric actin (c1) and low tropomyosin concentrations (ct) (c1/ct greater than 10), actin polymerization was not retarded by tropomyosin because actin polymerization was faster than binding of tropomyosin to actin filaments. At low actin concentrations and high tropomyosin concentrations (c1/ct less than 5), the rate of elongation of actin filaments was decreased because actin polymerization was slower than binding of tropomyosin at the ends of actin filaments. The results were quantitatively analyzed by a model in which it was assumed that actin-bound tropomyosin molecules which extend beyond the ends of actin filaments retard association of actin monomers with filament ends. Under the experimental conditions (100 mM KCl, 1 mM MgCl2, pH 7.5, 25 degrees C), the rate constant for binding of tropomyosin to actin filaments turned out to be about 2.5 X 10(6) to 4 X 10(6) M-1 S-1.
Wegner
A
A
Institute of Physiological Chemistry, Ruhr-University Bochum, Federal Republic of Germany.
Ruhnau
K
K
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D066298:In Vitro Techniques; D007700:Kinetics; D008956:Models, Chemical; D009132:Muscles / Q000378:metabolism; D011108:Polymers; D011817:Rabbits; D014335:Tropomyosin / Q000378:metabolism*
D000199:Actins; D011108:Polymers; D014335:Tropomyosin