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The N-terminal Domain of Pseudomonas aeruginosaExoenzyme S Is a GTPase-activating Protein for Rho GTPases
Open accessAbstract
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.
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The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants
Scheffzek, K., Ahmadian, M. R., Kabsch, W., Wiesmüller, L., Lautwein, A., Schmitz, F., & Wittinghofer, A. (1997) · Science · doi:10.1126/science.277.5324.333 · Cited by 1,543
Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases
Caron, E., & Hall, A. (1998) · Science · doi:10.1126/science.282.5394.1717 · Cited by 1,019
Cited by
Targeting mechanisms of Pseudomonas aeruginosa pathogenesis
Kipnis, E., Sawa, T., & Wiener-Kronish, J. (2006) · Médecine et Maladies Infectieuses · doi:10.1016/j.medmal.2005.10.007 · Cited by 353
Modulation of Host Signaling by a Bacterial Mimic
Stebbins, C. E., & Galán, J. E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00141-6 · Cited by 160
Metadata
- Authors
- Goehring, U.-M., Schmidt, G., Pederson, K. J., Aktories, K., & Barbieri, J. T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-12
- Volume
- 274
- Issue
- 51
- Pages
- 36369-36372
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2083861520
- Cited by
- 303
- References
- 2
- FWCI
- 6.09
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Goehring, U.-M., Schmidt, G., Pederson, K. J., Aktories, K., & Barbieri, J. T. (1999). The N-terminal Domain of Pseudomonas aeruginosaExoenzyme S Is a GTPase-activating Protein for Rho GTPases. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.51.36369
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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