The study provides direct evidence that ADP-Pi-F-actin is the major transient intermediate in ATP-actin polymerization.
Answers are grounded in this paper and cite their sources.
Supports ADP-Pi-F-actin as major polymerization intermediate; leaves open its role in cellular actin dynamics.
The sequence of reactions involved in the polymerization of ATP-actin and accompanying hydrolysis of ATP has been investigated by using a new glass-fiber filter assay. The assay allows the rapid separation of filaments from monomeric actin, and therefore the straightforward identification of the nucleotide bound to F-actin in the time course of polymerization, using double-labeled [gamma-32P,3H]ATP. The data bring a direct confirmation of the existence of the previously proposed ATP-F-actin intermediate in the time course of polymerization. Moreover, comparison of the hydrolyzed ATP (i.e., acid-labile [32P]Pi) and of 32P bound to F-actin provides direct evidence for the second intermediate ADP-Pi-F-actin in the polymerization process. This latter species is the major transient in the polymerization of ATP-actin, its lifetime being of the order of minutes.
No takes yet. Share an insight, caveat, or question.
Carlier et al. (1986) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: