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PMID: 6243744 Published · ppublish English Journal Article

(ADP-ribose)n participates in DNA excision repair.

Nature ·Vol. 283 ·No. 5747 ·1980-02-07 ·Pages 593-6

Durkacz BW, Omidiji O, Gray DA, Shall S

Abstract

Chromatin proteins are covalently modified by at least five different processes; in no case has the precise physiological function been established. One of these post-synthetic, covalent modifications is effected by the enzyme poly(ADP-ribose) polymerase, which uses the coenzyme NAD+ to ADP-ribosylate chromatin proteins. The modification consists largely of mono(ADP-ribose), but long, homopolymer chains of (ADP-ribose) are also present. Various physiological functions have been suggested for (ADP-ribose)n. Here we demonstrate that one function of (ADP-ribose)n is to participate in the cellular recovery from DNA damage. Specific inhibitors of poly(ADP-ribose) polymerase prevent rejoining of DNA strand breaks caused by dimethyl sulphate and cytotoxicity is enhanced thereby. The rejoining of strand breaks is prevented also by nutritionally depleting the cells of NAD.

MeSH Terms
ADP Ribose Transferases Alkylating Agents/pharmacology Animals Benzamides/pharmacology DNA Repair/drug effects Leukemia L1210 Mice NAD/metabolism NAD+ Nucleosidase/metabolism Nucleoside Diphosphate Sugars/metabolism Poly Adenosine Diphosphate Ribose/metabolism Poly(ADP-ribose) Polymerase Inhibitors Poly(ADP-ribose) Polymerases/metabolism
Chemicals
Alkylating Agents Benzamides Nucleoside Diphosphate Sugars Poly(ADP-ribose) Polymerase Inhibitors NAD Poly Adenosine Diphosphate Ribose ADP Ribose Transferases Poly(ADP-ribose) Polymerases NAD+ Nucleosidase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Durkacz B W
Omidiji O
Gray D A
Shall S
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1980-02-07
Pages
593-6
Language
English
Region
England
NLM ID
0410462
Subset
IM
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