ADP-ribosylation of p21ras and related proteins by Pseudomonas aeruginosa exoenzyme S.
Pseudomonas aeruginosa exoenzyme S ADP-ribosylates p21ras and several related proteins. ADP-ribosylation of p21ras does not alter interactions with guanine nucleotides. The ras-related GTP-binding proteins, including Rab3, Rab4, Ral, Rap1A, and Rap2, are also substrates; given these results, we propose a model for the role of exoenzyme S in pathogenesis.
Department of Molecular Biology and Microbiology, Tufts University Health Sciences Campus, Boston, Massachusetts 02111.
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Coburn
D M
DM
Gill
D036002:ADP Ribose Transferases; D001427:Bacterial Toxins; D019204:GTP-Binding Proteins / Q000378:metabolism*; D020690:GTPase-Activating Proteins; D006150:Guanine Nucleotides / Q000378:metabolism; D066298:In Vitro Techniques; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D016283:Proto-Oncogene Proteins p21(ras) / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D020703:ras GTPase-Activating Proteins
D001427:Bacterial Toxins; D020690:GTPase-Activating Proteins; D006150:Guanine Nucleotides; D011506:Proteins; D020703:ras GTPase-Activating Proteins; D036002:ADP Ribose Transferases; D011065:Poly(ADP-ribose) Polymerases; C444820:exoenzyme S; D019204:GTP-Binding Proteins; D016283:Proto-Oncogene Proteins p21(ras)