Effect of capping protein on the kinetics of actin polymerization

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Abstract
Acanthamoeba capping protein increased the rate of actin polymerization from monomers with and without Ca. In the absence of Ca, capping protein also increased the critical concentration for polymerization. Various models were evaluated for their ability to predict the effect of capping protein on kinetic curves for actin polymerization under conditions where the critical concentration was not changed. Several models, which might explain the increased rate of polymerization from monomers, were tested. Two models which predicted the experimental data poorly were capping protein, similar to an actin filament, (bypassing nucleation); and capping protein fragments. Three models in which capping protein accelerated, but did not bypass, nucleation predicted the data well. In the best one, capping protein resembled a nondissociable actin dimer. Several lines of evidence supported the idea that capping protein blocks the barbed end of actin filaments, preventing the addition and loss of monomers. This mechanism was also supported here by the effect of capping protein on the kinetics of actin polymerization which was nucleated by preformed actin filaments. Low capping protein concentrations slowed nucleated polymerization, presumably because capping protein blocked elongation at barbed ends of filaments. High capping protein concentrations accelerated nucleated polymerization because of capping protein''s ability to interact with monomers and accelerate nucleation.