ADP-ribosylation of actin causes increase in the rate of ATP exchange and inhibition of ATP hydrolysis.
ADP-ribosylation of skeletal muscle actin by Clostridium perfringens iota toxin increased the rate of exchange of actin-bound [gamma-32P]ATP by unlabelled ATP about twofold. Increased exchange rates were observed with ATP and ATP[gamma S], much less with ADP but not with AMP or NAD. ADP-ribosylation of skeletal muscle actin reduced "basal" and Mg2+ (1 mM)-induced ATP hydrolysis by about 80%. Similar inhibition of ATP hydrolysis was observed with liver actin ADP-ribosylated by Clostridium botulinum C2 toxin. The data indicate that ADP-ribosylation of actin at Arg-177 largely affects the ATP-binding and ATPase activity.
Geipel
U
U
Rudolf-Buchheim-Institut für Pharmakologie, Justus-Liebig-Universität Giessen, Federal Republic of Germany.
Just
I
I
Schering
B
B
Haas
D
D
Aktories
K
K
D036002:ADP Ribose Transferases; D000199:Actins / Q000378:metabolism* / Q000502:physiology; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D001427:Bacterial Toxins / Q000494:pharmacology; D001665:Binding Sites / Q000187:drug effects; D001905:Botulinum Toxins / Q000494:pharmacology; D003016:Clostridium perfringens; D006868:Hydrolysis; D008099:Liver / Q000187:drug effects / Q000378:metabolism; D008274:Magnesium / Q000494:pharmacology; D015636:Magnesium Chloride; D009132:Muscles / Q000187:drug effects / Q000378:metabolism; D011817:Rabbits; D013552:Swine
D000199:Actins; D001427:Bacterial Toxins; C050737:iota toxin, Clostridium perfringens; D015636:Magnesium Chloride; D000246:Adenosine Diphosphate Ribose; D000255:Adenosine Triphosphate; D036002:ADP Ribose Transferases; D001905:Botulinum Toxins; D000251:Adenosine Triphosphatases; D008274:Magnesium