PMID: 2505752Jul 1, 1989Paper

Demonstration and partial characterization of ADP-ribosylation in Pseudomonas maltophilia

The Biochemical Journal
C EdmondsA P Johnstone

Abstract

ADP-ribosylation of proteins occurs in many eukaryotes, and it is also the mechanism of action of a growing number of important bacterial toxins. To date, however, there is only one well-characterized ADP-ribosylation system where the ADP-ribosyltransferase and the substrate protein are both bacterial in origin, namely within the nitrogen-fixing bacterium Rhodospirillum rubrum. The present paper demonstrates the endogenous ADP-ribosylation of two proteins of Mr 32,000 and 20,000 within Pseudomonas maltophilia, a Gram-negative aerobe. The proteins have been partially purified: two apparently separate species of modified protein can be separated by ion-exchange chromatography and gel filtration (V0 and Mr 158,000 - Vi). The substrate protein(s) either has, or is co-eluted with, NAD+ glycohydrolase activity. The modification is mono-ADP-ribosyl in nature. The linkage between the acceptor amino acid and the ADP-ribose moiety is alkali-labile and stable to hydroxylamine, possibly indicating an S-glycosidic bond. The activity appears to be a true ADP-ribosylation reaction and not an NAD+ glycohydrolase activity followed by non-enzymic addition of ADP-ribose to protein. The results presented here indicate that ADP-ribosylation may hav...Continue Reading

Citations

Sep 3, 2013·Journal of Proteomics·Joel A CainStuart J Cordwell
Jul 1, 1997·Journal of Cellular Biochemistry·M R Faraone-MennellaB Farina
Jun 1, 1990·FEMS Microbiology Letters·A PenyigeJ C Ensign
Sep 1, 1994·Molecular and Cellular Biochemistry·P W Ludden
Jan 19, 1995·Biochimica Et Biophysica Acta·M R Faraone-MennellaB Farina
Apr 15, 1991·Biochemical and Biophysical Research Communications·G SomanR W Finberg

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