Lines of KB cells resistant to cytochalasin B have been isolated and characterized. The mutant Cyt 1 exhibits increased cross-resistance to cytochalasin E. Cyt 1 cells bind less cytochalasin B than parental KB cells. Two-dimensional gel analysis shows that Cyt 1 cells carry an alteration in beta-actin. This is further confirmed by one-dimensional peptide analysis. The altered beta-actin (beta'-actin) is synthesized when poly(A)+ RNA from Cyt 1 cells is translated in a reticulocyte-cell-free translation system. These results suggest that the primary site of action of cytochalasin B on cellular motility processes is beta-actin.
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