Role of poly(ADP-ribose) formation in DNA repair

Nature. 1992 Mar 26;356(6367):356-8. doi: 10.1038/356356a0.


The abundant nuclear enzyme poly(ADP-ribose) polymerase catalyses the synthesis of poly(ADP-ribose) from nicotinamide adenine dinucleotide (NAD+). This protein has an N-terminal DNA-binding domain containing two zinc-fingers, which is linked to the C-terminal NAD(+)-binding domain by a short region containing several glutamic acid residues that are sites of auto-poly(ADP-ribosyl)ation. The intracellular production of poly(ADP-ribose) is induced by agents that generate strand interruptions in DNA. The branched homopolymer chains may attain a size of 200-300 residues but are rapidly degraded after synthesis. The function of poly(ADP-ribose) synthesis is not clear, although it seems to be required for DNA repair. Here we describe a human cell-free system that enables the role of poly(ADP-ribose) synthesis in DNA repair to be characterized. The results indicate that unmodified polymerase molecules bind tightly to DNA strand breaks; auto-poly(ADP-ribosyl)ation of the protein then effects its release and allows access to lesions for DNA repair enzymes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Benzamides / pharmacology
  • Cell-Free System
  • DNA Damage
  • DNA Repair*
  • Histones / metabolism
  • Humans
  • In Vitro Techniques
  • NAD / metabolism
  • Poly Adenosine Diphosphate Ribose / physiology*
  • Poly(ADP-ribose) Polymerase Inhibitors
  • Poly(ADP-ribose) Polymerases / metabolism*


  • Benzamides
  • Histones
  • Poly(ADP-ribose) Polymerase Inhibitors
  • NAD
  • Poly Adenosine Diphosphate Ribose
  • 3-aminobenzamide
  • Poly(ADP-ribose) Polymerases