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
Date
05/25/1989Pubmed ID
2498323Scopus ID
2-s2.0-0024356764 (requires institutional sign-in at Scopus site) 97 CitationsAbstract
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 DMAuthor
Jenifer Coburn PhD Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
ADP Ribose TransferasesAnimals
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
