This chapter discusses poly ADP-ribosylation of protein. ADP-ribosylation is a postsynthetic modification of protein that involves the covalent attachment of the ADP-ribose moiety of NAD to specific amino-acid residues or to another ADP-ribose moiety to form a poly(ADP-ribose) molecule. There are two classes of enzymes responsible for this modification: (1) the mono(ADP-ribosyl) transferases and (2) poly(ADP-ribosyl) synthetases. Some bacterial toxins alter the activity of critical metabolic pathways by catalyzing the ADP-ribosylation of a key regulatory enzyme. Diphtheria toxin and Pseudomonas aeruginosa exotoxin A catalyze the mono ADP-ribosylation of eukaryotic elongation factor II, resulting in the inhibition of protein synthesis; choleragen and E. coli heat-labile enterotoxin catalyze the ADP-ribosylation of a regulatory protein of adenylate cyclase, resulting in the activation of the enzyme. Poly(ADP-ribose) synthetase is localized primarily in the nucleus of eukaryotic cells.
Pekala, P. H., & Moss, J. (1983). Poly ADP-Ribosylation of Protein. Current Topics in Cellular Regulation, 22(C), 1–49. https://doi.org/10.1016/B978-0-12-152822-5.50005-1