Poly ADP-Ribosylation of Protein

Citations of this article
Mendeley users who have this article in their library.
Get full text


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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free