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J Biol Chem, Vol. 274, Issue 14, 9503-9508, April 2, 1999

Pseudomonas aeruginosa Exoenzyme S, a Double ADP-ribosyltransferase, Resembles Vertebrate Mono-ADP-ribosyltransferases

Anand K. GanesanDagger , L. Mende-Mueller§, Jorg Selzer, and Joseph T. BarbieriDagger

From the Medical College of Wisconsin, Departments of Dagger  Microbiology and Molecular Genetics and § Biochemistry, Milwaukee, Wisconsin 53226 and the  Institute of Pharmacology and Toxicology, University of Freiburg, D-79104 Freiburg, Germany

Previous data indicated that Pseudomonas aeruginosa exoenzyme S (ExoS) ADP-ribosylated Ras at multiple sites. One site appeared to be Arg41, but the second site could not be localized. In this study, the sites of ADP-ribosylation of c-Ha-Ras by ExoS were directly determined. Under saturating conditions, ExoS ADP-ribosylated Ras to a stoichiometry of 2 mol of ADP-ribose incorporated per mol of Ras. Nucleotide occupancy did not influence the stoichiometry or velocity of ADP-ribosylation of Ras by ExoS. Edman degradation and mass spectrometry of V8 protease generated peptides of ADP-ribosylated Ras identified the sites of ADP-ribosylation to be Arg41 and Arg128. ExoS ADP-ribosylated the double mutant, RasR41K,R128K, to a stoichiometry of 1 mol of ADP-ribose incorporated per mol of Ras, which indicated that Ras possessed an alternative site of ADP-ribosylation. The alternative site of ADP-ribosylation on Ras was identified as Arg135, which was on the same alpha -helix as Arg128.

Arg41 and Arg128 are located within two different secondary structure motifs, beta -sheet and alpha -helix, respectively, and are spatially separated within the three-dimensional structure of Ras. The fact that ExoS could ADP-ribosylate a target protein at multiple sites, along with earlier observations that ExoS could ADP-ribosylate numerous target proteins, were properties that have been attributed to several vertebrate ADP-ribosyltransferases. This prompted a detailed alignment study which showed that the catalytic domain of ExoS possessed considerably more primary amino acid homology with the vertebrate mono-ADP-ribosyltransferases than the bacterial ADP-ribosyltransferases. These data are consistent with the hypothesis that ExoS may represent an evolutionary link between bacterial and vertebrate mono-ADP-ribosyltransferases.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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