Abstract
Publisher Summary ADP-ribosylation involves a group of posttranslational modifications of proteins in which the ADP-ribose moiety of NAD is transferred to various protein acceptors. The ADP-ribose transferred remains monomeric or is polymerized, which allows the classification of mono(ADP-ribosyl)ation and poly(ADP-ribosyl)ation. This chapter discusses the various mono- and poly(ADP-ribosyl)ation reactions. Many of the enzymes catalyzing mono(ADP-ribosyl)ation are microbial toxins such as diphtheria toxin, cholera toxin, and Escherichia coli enterotoxin, whereas their targets are eukaryotic enzymes such as elongation factor 2 and a guanine nucleotide regulatory component of the adenylate cyclase system. On the other hand, poly(ADP-ribosyl)ation involves almost exclusively enzymes as well as acceptors of eukaryotic origin. Mono- and poly(ADP-ribosyl)ation are further different in the reversibility of the reaction and the nature of ADP-ribosyl protein linkages (N-glycosides versus O-glycosides). The chapter discusses the present knowledge of and recent results on poly(ADP-ribosyl)ation reactions. The biosynthesis of poly(ADP-ribosyl) protein is reconstituted in vitro with purified synthetase preparations.
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