The mechanism of ATP hydrolysis by polymer actin.
The rate of actin polymerization, the rate of nucleotide splitting and the rate of the nucleotide exchange have been measured simultaneously. Correlation of these three measurements demonstrated that nucleotide splitting and exchange were mainly connected with the association and dissociation reactions of actin protomers at the ends of actin filaments and were not caused by release and rebinding of nucleotide molecules at the binding sites along the filament. The observation made by others that the nucleotide exchange was accelerated in the presence of ATP was explained by the translocational head-to-tail polymerization of actin: Due to the simultaneous lengthening of the filament at one end and shortening at the other, nucleotide molecules are incorporated at one end and released at the other. In the absence of ATP, where the head-to-tail polymerization mechanism was not operative nucleotide exchange was brought about by the slow process of length fluctuation of polymers.
D000199:Actins / Q000378:metabolism; D000244:Adenosine Diphosphate; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008027:Light; D046911:Macromolecular Substances; D008433:Mathematics; D011485:Protein Binding; D012542:Scattering, Radiation
D000199:Actins; D046911:Macromolecular Substances; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases