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The polymerization of actin filaments is coupled to the hydrolysis ofadenosine triphosphate (ATP), which involves both the cleavage of ATP and therelease of inorganic phosphate. We describe hydrolysis by a reduced two-statemodel with a cooperative cleavage mechanism, where the cleavage rate depends onthe state of the neighboring actin protomer in a filament. We obtaintheoretical predictions of experimentally accessible steady state quantitiessuch as the size of the ATP-actin cap, the size distribution of ATP-actinislands, and the cleavage flux for cooperative cleavage mechanisms.

Coupling of actin hydrolysis and polymerization: Reduced description with two nucleotide states