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J Biol Chem, Vol. 274, Issue 51, 36369-36372, December 17, 1999
,§,
,§, and
From the Pseudomonas aeruginosa exoenzyme S
(ExoS) is a bifunctional cytotoxin. The ADP-ribosyltransferase domain
is located within the C terminus part of ExoS. Recent studies showed
that the N terminus part of ExoS (amino acid residues 1-234,
ExoS(1-234)), which does not possess ADP-ribosyltransferase activity,
stimulates cell rounding when transfected or microinjected into
eukaryotic cells. Here we studied the effects of ExoS(1-234) on
nucleotide binding and hydrolysis by Rho GTPases. ExoS(1-234)
(100-500 nM) did not influence nucleotide exchange of Rho,
Rac, and Cdc42 but increased GTP hydrolysis. A similar increase in
GTPase activity was stimulated by full-length ExoS. Half-maximal
stimulation of GTP hydrolysis by Rho, Rac, and Cdc42 was observed at
10-11 nM ExoS(1-234), respectively. We identified
arginine 146 of ExoS to be essential for the stimulation of GTPase
activity of Rho proteins. These data identify ExoS as a
GTPase-activating protein for Rho GTPases.
Institut für Pharmakologie und
Toxikologie, Albert-Ludwigs-Universität Freiburg, D-79104
Freiburg, Germany and ¶ Medical College of Wisconsin, Microbiology
and Molecular Genetics, Milwaukee, Wisconsin 53226
Supported by National Institutes of Health Grant AI10017 (NIAID).
**
Supported by National Institutes of Health Grant AI30162 (NIAID).
To whom correspondence should be addressed: Medical College of
Wisconsin, Microbiology and Molecular Genetics, 8701 Watertown Plank
Rd., Milwaukee, WI 53226. Tel.: 414-456-8412; Fax: 414-456-6535; E-mail: toxin@mcw.edu.
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