ADP-ribosylation of actin by Clostridium perfringens iota toxin and turkey erythrocyte ADP-ribosyltransferase A: effects on profilin-regulated nucleotide exchange and ATPase activity

Naunyn Schmiedebergs Arch Pharmacol. 1996 Dec;354(6):693-7. doi: 10.1007/BF00166893.

Abstract

Effects of ADP-ribosylation of skeletal muscle alpha-actin by Clostridium perfringens iota toxin and by turkey erythrocyte ADP-ribosyltransferase A on profilin-regulated nucleotide exchange and ATPase activity were compared. ADP-ribosylation of actin at Arg 177 by Clostridium perfringens iota toxin increased the nucleotide dissociation rate from 2.2 x 10(-3) s-1 to 4.5 x 10(-3) s-1 without affecting the profilin-induced stimulation of nucleotide exchange. In contrast, ADP-ribosylation of actin at Arg95/Arg372 induced by turkey erythrocyte transferase decreased the nucleotide dissociation rate to 1.5 x 10(3) s-1 and inhibited the profilin-induced stimulation of nucleotide exchange. Whereas toxin-induced ADP-ribosylation at Arg177 blocked actin ATPase, basal G-actin ATPase was not altered by ADP-ribosylation at Arg95/Arg372 but inhibited profilin effects on actin ATPase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADP Ribose Transferases*
  • Actins / metabolism*
  • Adenosine Diphosphate Ribose / metabolism*
  • Adenosine Triphosphatases / metabolism*
  • Adenosine Triphosphate / metabolism
  • Animals
  • Bacterial Toxins / pharmacology*
  • Cattle
  • Clostridium perfringens / pathogenicity*
  • Contractile Proteins*
  • Erythrocytes / enzymology*
  • Microfilament Proteins / pharmacology*
  • Poly(ADP-ribose) Polymerases / physiology*
  • Profilins
  • Rabbits
  • Turkeys

Substances

  • Actins
  • Bacterial Toxins
  • Contractile Proteins
  • Microfilament Proteins
  • Profilins
  • iota toxin, Clostridium perfringens
  • Adenosine Diphosphate Ribose
  • Adenosine Triphosphate
  • ADP Ribose Transferases
  • Poly(ADP-ribose) Polymerases
  • Adenosine Triphosphatases