Demonstrates that the ATP hydrolysis step during actin polymerization is essentially irreversible due to a large decrease in free energy.
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Updates actin assembly energetics in muscle cells; leaves open relevance to human cardiac remodeling or contractility.
The hydrolysis of ATP that accompanies the polymerization of actin occurs on the F-actin subsequent to the addition of the G-ATP-actin subunit to the elongating filament. We now show that this ATP hydrolysis is essentially irreversible. Thus, a large decrease in free energy occurs at the cleavage step, F-ATP-actin----F-ADP-Pi-actin.
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Carlier et al. (1988) studied this question.
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