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Several GTP-binding proteins, including p21c-H-ras, are preferred substrates of Pseudomonas aeruginosa exoenzyme S. J Biol Chem 1989 May 25;264(15):9004-8 PMID: 2498323

Pubmed ID

2498323

Abstract

Pseudomonas aeruginosa exoenzyme S has appeared to be relatively indiscriminate in its choice of substrates, but in fact it ADP-ribosylates only a small subset of cellular proteins and exhibits a marked preference for several different membrane-associated proteins of apparent Mr = 23,000-25,000, at least some of which appear to bind GTP. One of these is the p21 product of the proto-oncogene c-H-ras, which can be labeled to completion. ADP-ribosylation does not alter the interaction of p21c-H-ras with guanyl nucleotides, but does cause a shift in electrophoretic mobility that implies a large conformational change. Exoenzyme S modifies all of its substrates at arginine residues.

Author List

Coburn J, Wyatt RT, Iglewski BH, Gill DM

Author

Jenifer Coburn PhD Professor in the Medicine department at Medical College of Wisconsin




Scopus

2-s2.0-0024356764   89 Citations

MESH terms used to index this publication - Major topics in bold

ADP Ribose Transferases
Animals
Bacterial Toxins
Cells, Cultured
Columbidae
Electrophoresis, Gel, Two-Dimensional
Erythrocyte Membrane
GTP-Binding Proteins
Kinetics
Membrane Proteins
Mice
Molecular Weight
Poly(ADP-ribose) Polymerases
Proto-Oncogene Proteins
Proto-Oncogene Proteins p21(ras)
Pseudomonas aeruginosa
Substrate Specificity
jenkins-FCD Prod-332 f92a19b0ec5e8e1eff783fac390ec127e367c2b5