Cholera Toxin Can Catalyze ADP-Ribosylation of Cytoskeletal Proteins

Cholera toxin catalyzes transfer of radiolabel from [32P]NAD+to several peptides in particulate preparations of human foreskin fibroblasts. Resolution of these peptides by two-dimensional gel electrophoresis allowed identification of two peptides of Mr= 42,000 and 52,000 as peptide subunits of a regulatory component of adenylate cyclase. The radiolabeling of another group of peptides (Mr= 50,000 to 65,000) suggested that cholera toxin could catalyze ADP-ribosylation of cytoskeletal proteins. This suggestion was confirmed by showing that incubation with cholera toxin and [32P]NAD+caused radiolabeling of purified microtubule and intermediate filament proteins.