Nonmuscle actin ADP-ribosylated by botulinum C2 toxin caps actin filaments.
The effect of nonmuscle actin ADP-ribosylated by botulinum C2 toxin on the polymerization of nonmuscle actin was investigated in order to clarify whether nonmuscle actin is converted into a capping protein by ADP-ribosylation. ADP-ribosylated actin was found to decrease the rate of polymerization of actin filaments which are free at both ends. ADP-ribosylated actin turned out to have no effect on the rate or extent of polymerization at the pointed ends of actin filaments the barbed ends of which were capped by gelsolin. The monomer concentration reached at the final stage of polymerization was similar to the critical concentration of the pointed ends of actin filaments. The results suggest that nonmuscle actin ADP-ribosylated by botulinum C2 toxin acts as a capping protein which binds to the barbed ends to inhibit polymerization.
Weigt
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C
Institute of Physiological Chemistry, Ruhr-University Bochum, FRG.
Just
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I
Wegner
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A
Aktories
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K
D051339:Actin Depolymerizing Factors; D000199:Actins / Q000378:metabolism* / Q000494:pharmacology; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D001905:Botulinum Toxins / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000378:metabolism; D051345:Destrin; D018260:Gelsolin; D007700:Kinetics; D008840:Microfilament Proteins / Q000378:metabolism / Q000494:pharmacology; D011108:Polymers; D013552:Swine
D051339:Actin Depolymerizing Factors; D000199:Actins; D002135:Calcium-Binding Proteins; D051345:Destrin; D018260:Gelsolin; D008840:Microfilament Proteins; D011108:Polymers; D000246:Adenosine Diphosphate Ribose; D001905:Botulinum Toxins