EFFECT OF ATP ON ACTIN FILAMENT STIFFNESS

ACTIN is an adenine nucleotide-binding protein and an ATPase1. The bound adenine nucleotide stabilizes the protein against denaturation2 and the ATPase activity, although not required for actin polymerization, affects the kinetics of this assembly (see ref. 3 for review). Here we provide evidence for another effect of adenine nucleotides. We find that actin filaments made from ATP-containing monomers, the ATPase activity of which hydrolyses ATP to ADP following polymerization, are stiff rods, whereas filaments prepared from ADP-monomers are flexible. ATP exchanges with ADP in such filaments and stiffens them. Because both kinds of actin filaments contain mainly ADP, we suggest the alignment of actin monomers in filaments that have bound and hydrolysed ATP traps them conformationally and stores elastic energy. This energy would be available for release by actin-binding proteins that transduce force or sever actin filaments. These data support earlier proposals that actin is not merely a passive cable, but has an active mechanochemical role in cell function4-6. © 1990 Nature Publishing Group.