Home
  >  
Section 9
  >  
Chapter 8,088

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

Sehr, P.; Just, I.; Aktories, K.

Naunyn-Schmiedeberg's Archives of Pharmacology 354(6): 693-697

1996


ISSN/ISBN: 0028-1298
PMID: 8971727
DOI: 10.1007/bf00166893
Accession: 008087030

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 Arg177 by Clostridium perfringens iota toxin increased the nucleotide dissociation rate from 2.2 times 10-3 s-1 to 4.5 times 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 times 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.

PDF emailed within 0-6 h: $19.90