The polymerization reaction of muscle actin.
Recent advances in the studies of the aggregation of G-actin monomers, containing one molecule of ATP, to long filaments of F-actin, with a concomitant hydrolysis of the nucleotide to ADP, are reviewed. With the aid of omega-ATP, the association and dissociation rate constant of the nucleotide could be determined. The binding of the nucleotide is enhanced by the binding of one Ca++ ion, probably at a different site. The delta G value of the Mg++ or Ca++ induced polymerization has been determined to --39 to--59 kJ/mole, the critical protein concentration for the ATP-G-actin to ADP-F-actin conversion is very strongly influenced by the concentration of bivalent cations. The rate constants of the protein monomers, and the rate and equilibrium constants for the propagation step show the process to be extremely cooperative. Actin shows the interesting phenomenon of translocational head-to-tail polymerization, which may be regulated by ATP. The contact sites between the monomers in F-actin have been labeled by chemical modification. Two tryosine residues, 53 and 69, are probably close to one of the two sites. The ATP binding sites has been labeled by an ATP analog, and there is evidence that it is close to the contact site.
D000199:Actins / Q000378:metabolism*; D000227:Adenine Nucleotides / Q000378:metabolism*; D000345:Affinity Labels; D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D009132:Muscles / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism; D011487:Protein Conformation; D014335:Tropomyosin / Q000378:metabolism
D000199:Actins; D000227:Adenine Nucleotides; D000345:Affinity Labels; D014335:Tropomyosin; D009218:Myosins