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ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin

Schering, B.; Bärmann, M.; Chhatwal, G.S.; Geipel, U.; Aktories, K.

European Journal of Biochemistry 171(1-2): 225-229

1988


ISSN/ISBN: 0014-2956
PMID: 2892681
DOI: 10.1111/j.1432-1033.1988.tb13780.x
Accession: 039137420

The enzymatically active component ia of Clostridium perfringens iota toxin ADP-ribosylated actin in human platelet cytosol and purified platelet beta/gamma-actin, in a similar way to that been reported for component I of botulinum C2 toxin. ADP-ribosylation of cytosolic and purified actin by either toxin was inhibited by 0.1 mM phalloidin indicating that monomeric G-actin but not polymerized F-actin was the toxin substrate. Perfringens iota toxin and botulinum C2 toxin were not additive in ADP-ribosylation of platelet actin. Treatment of intact chicken embryo cells with botulinum C2 toxin decreased subsequent ADP-ribosylation of actin in cell lysates by perfringens iota or botulinum C2 toxin. In contrast to botulinum C2 toxin, perfringens iota toxin ADP-ribosylated skeletal muscle alpha-actin with a potency and efficiency similar to non-muscle actin. ADP-ribosylation of purified skeletal muscle and non-muscle actin by perfringens iota toxin led to a dose-dependent impairment of the ability of actin to polymerize.

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