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.
Albert Ludwigs Universitat Freiburg, Institut fur Experimentelle & Klinische Pharmakologie & Toxikologie, Germany.
Gerd
G
Haug
Holger
H
Barth
Klaus
K
Aktories
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