Purification and activity of the Rho ADP-ribosylating binary C2/C3 toxin.
C3 exoenzyme from Clostridium limosum, specifically ADP-ribosylates and inactivates Rho GTPases, but not or much less than Rac and Cdc42. To bypass the poor cell accessibility of the exoenzyme, a chimeric fusion toxin was constructed consisting of C3 exoenzyme and the N-terminal adaptor domain of the enzyme component C2I of the actin-ADP-ribosylating Clostridium botulinum C2 toxin. This fusion toxin C2IN-C3 is transported into cells by interaction with the binding and translocation component (C2II) of C2 toxin. Purification and activity of the chimeric toxin is reported.
Haug
Gerd
G
Albert Ludwigs Universitat Freiburg, Institut fur Experimentelle & Klinische Pharmakologie & Toxikologie, Germany.
Barth
Holger
H
Aktories
Klaus
K
D036002:ADP Ribose Transferases / Q000302:isolation & purification* / Q000378:metabolism*; D000818:Animals; D001905:Botulinum Toxins / Q000302:isolation & purification* / Q000378:metabolism*; D016466:CHO Cells; D006224:Cricetinae; D006367:HeLa Cells; D006801:Humans; D050506:Mutant Chimeric Proteins / Q000302:isolation & purification / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification / Q000378:metabolism; D020741:rho GTP-Binding Proteins / Q000378:metabolism
D050506:Mutant Chimeric Proteins; D011993:Recombinant Fusion Proteins; D036002:ADP Ribose Transferases; C063007:exoenzyme C3, Clostridium botulinum; D001905:Botulinum Toxins; D020741:rho GTP-Binding Proteins; C096324:botulinum toxin type C