Open AccessDe‐ADP‐ribosylation actin by Clostridium perfringens iota‐toxin and Clostridium botulinum C2 toxin
Author(s) -
JUST Ingo,
GEIPEL Udo,
WEGNER Albrecht,
AKTORIES Klaus
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb19282.x
Subject(s) - clostridium perfringens , toxin , adp ribosylation , clostridium botulinum , botulinum toxin , clostridium , microbiology and biotechnology , clostridiaceae , chemistry , biology , bacteria , biochemistry , genetics , enzyme , nad+ kinase , neuroscience
The reverse reaction of the ADP‐ribosylation of actin by Clostridium botulinum C2 toxin and Clostridium perfringens iota‐toxin was studied. In the presence of nicotinamide (30–50 mM) C2 toxin and iota‐toxin decreased the radioactive labeling of [ 32 P]ADP‐ribosylated actin and catalyzed the formation of [ 32 P]NAD. The pH optima for both reactions were 5.5 – 6.0. Concomitant with the removal of ADP–ribose, the ability of actin to polymerize was restored and actin ATPase activity increased. Neither ADP–ribosylation nor removal of ADP–ribose was observed after treatment of actin with EDTA, indicating that the native structure of actin is required for both reactions. ADP–ribosylation of platelet actin by C2 toxin was reversed by iota–toxin, confirming recent reports that both toxins modify the same amino acid in actin. However, C. botulinum C2 toxin was not able to cleave ADP–ribose from skeletal muscle actin which had been incorporated by iota–toxin, corroborating the different substrate specificities of both toxins.