Protein ADP-Ribosylation
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ADP-ribosylation of proteins was originally discovered in 1966 by Chambon et al. (1966), who detected polymers of ADP-ribose
attached to protein substrates. Since that time, protein ADP-ribosylation has been identified in a diverse range of species,
from bacteria to human, as well as within virtually every cellular compartment (Hilz et al., 1984; Ueda and Hayaishi, 1985;
Ogura et al, 1990; Williamson and Moss, 1990; Aktories and Wegner, 1992). In general, ADP-ribosylation is a posttranslational
modification in which one or more ADP-ribose moieties are transferred from a nicotinamide adenine dinucleotide (NAD+
) donor to an amino acid acceptor. It is important to note that NAD+
is a substrate in this process rather than a cofactor as it is in many enzyme reactions.
