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