Inhibition of cytochalasin D-stimulated G-actin ATPase by ADP-ribosylation with Clostridium perfringens iota toxin

Biochem J. 1990 Mar 1;266(2):335-9. doi: 10.1042/bj2660335.

Abstract

Clostridium perfringens iota toxin belongs to a novel family of actin-ADP-ribosylating toxins. The effects of ADP-ribosylation of skeletal muscle actin by Clostridium perfringens iota toxin on cytochalasin D-stimulated actin ATPase activity was studied. Cytochalasin D stimulated actin-catalysed ATP hydrolysis maximally by about 30-fold. ADP-ribosylation of actin completely inhibited cytochalasin D-stimulated ATP hydrolysis. Inhibition of ATPase activity occurred at actin concentrations below the critical concentration (0.1 microM), at low concentrations of Mg2+ (50 microM) and even in the actin-DNAase I complex, indicating that ADP-ribosylation of actin blocks the ATPase activity of monomeric actin and that the inhibitory effect is not due to inhibition of the polymerization of actin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADP Ribose Transferases*
  • Actins / metabolism*
  • Adenosine Diphosphate / metabolism
  • Adenosine Diphosphate Ribose / metabolism*
  • Adenosine Triphosphatases / antagonists & inhibitors*
  • Adenosine Triphosphate / metabolism
  • Animals
  • Bacterial Toxins / pharmacology*
  • Clostridium perfringens
  • Cytochalasin D / pharmacology*
  • Deoxyribonuclease I / metabolism
  • Dose-Response Relationship, Drug
  • In Vitro Techniques
  • Kinetics
  • Macromolecular Substances
  • Protein Binding
  • Rabbits

Substances

  • Actins
  • Bacterial Toxins
  • Macromolecular Substances
  • iota toxin, Clostridium perfringens
  • Adenosine Diphosphate Ribose
  • Cytochalasin D
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • ADP Ribose Transferases
  • Deoxyribonuclease I
  • Adenosine Triphosphatases