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Clostridium perfringens iota toxin ADP‐ribosylates skeletal muscle actin in Arg‐177
Author(s) -
Vandekerckhove Joël,
Schering Beate,
Bärmann Michael,
Aktories Klaus
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81129-8
Subject(s) - clostridium perfringens , thermolysin , actin , skeletal muscle , clostridium difficile toxin b , biochemistry , adp ribosylation , toxin , chemistry , biology , trypsin , clostridium difficile toxin a , bacteria , enzyme , anatomy , nad+ kinase , genetics , clostridium difficile , antibiotics
Clostridium perfringens iota toxin ADP‐ribosylates actin. Substrates of C. perfringens toxin are both non‐muscle β/γ‐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 [ 32 P]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.