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J. Biol. Chem., Vol. 276, Issue 12, 9537-9542, March 23, 2001
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From the Clostridium botulinum C3 is the
prototype of the family of the C3-like transferases that ADP-ribosylate
exclusively RhoA, -B and -C. The ADP-ribose at Asn-41 results in
functional inactivation of Rho reflected by disaggregation of the actin
cytoskeleton. We report on a new C3-like transferase produced by a
pathogenic Staphylococcus aureus strain. The transferase
designated C3Stau was cloned from the genomic DNA. At the
amino acid level, C3Stau revealed an identity of 35% to C3
from C. botulinum and Clostridium limosum
exoenzyme, respectively, and of 78% to EDIN from S. aureus. In addition to RhoA, which is the target of the other
C3-like transferases, C3Stau modified RhoE and Rnd3. RhoE
was ADP-ribosylated at Asn-44, which is equivalent to Asn-41 of RhoA.
RhoE and Rnd3 are members of the Rho subfamily, which are deficient in
intrinsic GTPase activity and possess a RhoA antagonistic cell
function. The protein substrate specificity found with recombinant Rho
proteins was corroborated by expression of RhoE in Xenopus
laevis oocytes showing that RhoE was also modified in
vivo by C3Stau but not by C3 from C. botulinum. The poor cell accessibility of C3Stau was
overcome by generation of a chimeric toxin recruiting the cell entry
machinery of C. botulinum C2 toxin. The chimeric
C3Stau caused the same morphological and cytoskeletal
changes as the chimeric C. botulinum C3. C3Stau
is a new member of the family of the C3-like transferases but is also
the prototype of a subfamily of RhoE/Rnd modifying transferases.
A Novel C3-like ADP-ribosyltransferase from
Staphylococcus aureus Modifying RhoE and Rnd3*
,,, and¶
Institut für Experimentelle und
Klinische Pharmakologie und Toxikologie der Universität
Freiburg, Hermann-Herder-Strasse 5, D-79104 Freiburg, the
§ GBF (German Research Center for Biotechnology),
Mascheroder Weg 1, D-38124 Braunschweig, and the ¶ Institut
für Toxikologie der Medizinischen Hochschule Hannover,
Carl-Neuberg-Strasse 1, D-30625 Hannover, Germany
*
This work was supported by Deutsche Forschungsgemeinschaft
Grant SFB 388 and Project Ak6/10.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.
To whom correspondence should be addressed: Tel.:
49-511-532-2812; Fax: 49-511-532-2879; E-mail:
just.ingo@mh-hannover.de.
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