NH2-terminal processing of Dictyostelium discoideum actin in vitro

the NHz- terminal acetyl and methionyl residues from the poly- peptide chain to generate a polypeptide terminating in aspartic acid. Removal of the methionine apparently requires its prior acetylation. Once the aspartic acid residue is exposed at the NHz terminus, the actin can again be acetylated in an acetyl-CoA-dependent reac- tion to yield a polypeptide probably identical with