Characterization of yeast‐expressed β‐actins, site‐specifically mutated at the tumor‐related residue Gly245

Abstract

The tumorigenic cell line HUT14 expresses a beta-actin carrying a mutation at position 245. In this study, two mutant beta-actins with amino acid changes at position 245 replacing the wild-type glycine by an aspartic acid and a lysine residue, respectively, were produced in the yeast Saccharomyces cerevisiae, purified to homogeneity and characterized with respect to polymerization behaviour and interaction with myosin. The major functional effect of these mutations appears to be an impaired polymerization, while the interaction with myosin seems less influenced. In addition, the results also suggest the presence of a Ca(2+)-binding site in the region of residue 245 in actin.