Polymerization of Acanthamoeba actin. Kinetics, thermodynamics, and co-polymerization with muscle actin.
The kinetics and thermodynamics for the polymerization of purified Acanthamoeba actin were studied and compared to muscle actin. Polymerization was qualitatively similar for the two actins with a rate-limiting nucleation step followed by rapid polymer extension. Polymerization occurred only above a threshold critical concentration which varied with polymerization conditions for each actin. In the presence of 2 mM MgCl2, nucleation of both actins was rapid and their critical concentrations were similarly low and not detectably dependent on temperature. In 0.1 M KCl, the rates of nucleation of both actins were much slower than when Mg2+ was present and were significantly different from each other. Also, under these conditions, the critical concentrations of Acanthamoeba and muscle actin were significantly different and both varied markedly with temperature. These quantitative differences between the two actins could be attributed to differences in both their enthalpies and entropies of polymerization, Acanthamoeba actin having the more positive deltaH and delta S. Co-polymerization of the two actins was also demonstrated. Overall, however, there were no qualitative differences between Acanthamoeba and muscle actin that would suggest a unique role for the monomer-polymer equilibrium of cytoplasmic actin in cell motility.
D000199:Actins / Q000378:metabolism; D000656:Amoeba / Q000378:metabolism*; D000818:Animals; D007700:Kinetics; D046911:Macromolecular Substances; D008274:Magnesium; D009132:Muscles / Q000378:metabolism; D011189:Potassium Chloride; D011485:Protein Binding; D011817:Rabbits; D013816:Thermodynamics
D000199:Actins; D046911:Macromolecular Substances; D011189:Potassium Chloride; D008274:Magnesium