ADP-ribose. A historical overview.
ADP-ribosylation of proteins was first detected as a modification of nuclear proteins by polymeric ADP-ribose residues derived from NAD+. Subsequently, the field developed into three destinct sections: (i) Possible function(s) of poly-ADP-ribosylation with increasing evidence for participation in DNA excision repair and perhaps in DNA recombination; (ii) Mono-ADP-ribosylation as a mechanism to inactivate (by some toxins) or to regulate enzymes/proteins (e.g. in bacterial nitrogen fixation, in protein traffic through membranes, in intercellular communication); (iii) Intramolecular ADP-ribosylation converting NAD+ to cyclic ADP-ribose, a possible Ca(2+)-mobilizing agonist. Thus, NAD+ first known as a cofactor of oxidoreductases has experienced an impressive metamorphosis from a housekeeping coenzyme to a multifunctional group transfering metabolite involved in an increasing number of intracellular and intercellular regulatory loops.
Hilz
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Institut für Physiologische Chemie, Universitätskrankenhaus Eppendorf, Hamburg, Germany.
D000246:Adenosine Diphosphate Ribose / Q000031:analogs & derivatives / Q000266:history* / Q000378:metabolism; D000818:Animals; D036563:Cyclic ADP-Ribose; D049673:History, 20th Century; D006801:Humans; D011064:Poly Adenosine Diphosphate Ribose / Q000378:metabolism
D036563:Cyclic ADP-Ribose; D000246:Adenosine Diphosphate Ribose; D011064:Poly Adenosine Diphosphate Ribose