FEBS Letters · 1987 · 179 citations · 15 references
Life SciencesBiochemistryMicrobiologyCytoskeletonEnzymologyProtein BiochemistryActin FilamentsBacterial ToxinsCytoskeletal Associated ProteinsMuscle PhysiologyProtein StructureProteolytic ProcessingAmino Acid Composition AnalysisBotulinum ToxinsClostridium PerfringensDigestionPeptide ProfileProtein ToxinsSkeletal Muscle Physiology
Clostridium perfringens iota toxin ADP-ribosylates actin. Substrates of C. perfringens toxin are both non-muscle beta/gamma-actin and skeletal muscle actin. This finding suggests that C. perfringens iota ADP-ribosylates the same amino acid in skeletal muscle and non-muscle actin as does C. botulinum C2 toxin in non-muscle actin. Protein chemical analysis involving thermolysin cleavage on [32P]ADP-ribosylated actin or tryptic digestion followed by a secondary thermolysin cleavage of the radiolabelled fragments showed one major site of ADP-ribosylation. From its amino acid composition and sequence, the radiolabelled peptide was identified as peptide 175-177, locating the acceptor ADP-ribosyl amino acid as Arg-177.
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