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J Biol Chem, Vol. 274, Issue 39, 27407-27414, September 24, 1999
From the Institut für Pharmakologie und Toxikologie
der Albert-Ludwigs-Universität Freiburg, Hermann-Herder-Strasse
5, D-79104 Freiburg, Germany
Clostridium botulinum exoenzyme C3
inactivates the small GTPase Rho by ADP-ribosylation. We used a C3
fusion toxin (C2IN-C3) with high cell accessibility to study the
kinetics of Rho inactivation by ADP-ribosylation. In primary cultures
of rat astroglial cells and Chinese hamster ovary cells, C2IN-C3
induced the complete ADP-ribosylation of RhoA and concomitantly the
disassembly of stress fibers within 3 h. Removal of C2IN-C3 from
the medium caused the recovery of stress fibers and normal cell
morphology within 4 h. The regeneration was preceded by the
appearance of non-ADP-ribosylated RhoA. Recovery of cell morphology was
blocked by the proteasome inhibitor lactacystin and by the translation
inhibitors cycloheximide and puromycin, indicating that intracellular
degradation of the C3 fusion toxin and the neosynthesis of Rho were
required for reversal of cell morphology. Escherichia coli
cytotoxic necrotizing factor CNF1, which activates Rho by deamidation
of Gln63, caused reconstitution of stress fibers and cell
morphology in C2IN-C3-treated cells within 30-60 min. The effect of
CNF1 was independent of RhoA neosynthesis and occurred in the presence of completely ADP-ribosylated RhoA. The data show three novel findings;
1) the cytopathic effects of ADP-ribosylation of Rho are rapidly
reversed by neosynthesis of Rho, 2) CNF1-induced deamidation activates
ADP-ribosylated Rho, and 3) inhibition of Rho activation but not
inhibition of Rho-effector interaction is a major mechanism underlying
inhibition of cellular functions of Rho by ADP-ribosylation.
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