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J. Biol. Chem., Vol. 277, Issue 17, 14771-14776, April 26, 2002
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From the Institut für Experimentelle und Klinische
Pharmakologie und Toxikologie der Albert-Ludwigs-Universität
Freiburg, Otto-Krayer-Haus, Albertstrasse 25, D-79104 Freiburg, the
¶ Institut für Toxikologie, Medizinische Hochschule
Hannover, D-30625 Hannover, and § Institut für
Pharmakologie, Universitätsklinikum Essen,
D-45122 Essen, Germany
RhoA, -B, and -C are ADP-ribosylated and
biologically inactivated by Clostridium botulinum C3
exoenzyme and related C3-like transferases. We report that RalA GTPase,
which is not ADP-ribosylated by C3, inhibits ADP-ribosylation of RhoA
by C3 from C. botulinum (C3bot), Clostridium
limosum (C3lim), and Bacillus cereus (C3cer) but not
from Staphylococcus aureus (C3stau) in human platelet membranes and rat brain lysate. Inhibition by RalA occurs with the GDP-
and guanosine 5'-3-O-(thio)triphosphate-bound forms of RalA
and is overcome by increasing concentrations of C3. A direct interaction of RalA with C3 was verified by precipitation of the transferase with GST-RalA-Sepharose. The affinity constant
(Kd) of the binding of RalA to C3lim was 12 nM as determined by fluorescence titration. RalA increased
the NAD glycohydrolase activity of C3bot by about 5-fold. Although RalA
had no effect on glucosylation of Rho GTPases by Clostridium
difficile toxin B, C3bot and C3lim inhibited glucosylation of
RalA by Clostridium sordellii lethal toxin. Furthermore,
C3bot decreased activation of phospholipase D by RalA. The data
indicate that several C3 exoenzymes directly interact with RalA without
ADP-ribosylating the GTPase. The interaction is of high affinity and
interferes with essential functions of C3 and RalA.
Interaction of the Rho-ADP-ribosylating C3 Exoenzyme with
RalA*
,
*
This work was supported by the Deutsche
Forschungsgemein-schaft (Sonderforschungsbereich 388).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Deutsches Krebsforschungszentrum Im
Neuenheimer Feld 280, D-69120 Heidelberg, Germany.
To whom correspondence should be addressed: Institut für
Pharmakologie und Toxikologie der Albert-Ludwigs-Universität
Freiburg Otto-Krayer-Haus, Albertstr. 25, D-79104 Freiburg. Tel.:
761-203-5301; Fax: 761-203-5311; E-mail:
aktories@ruf.uni-freiburg.de.
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