The inhibitory effect of Zn2+ on poly(ADP-ribose) polymerase activity and its reversal.
Zn2+ inhibits purified poly(ADP-ribose) polymerase (50% inhibition at 10 microM). Furthermore poly (ADP-ribose) polymerase present in nuclei and metaphase chromosome clusters is also inhibited by Zn2+. The inactivated enzyme could be re-activated by dithiothreitol. The concentration of Zn2+ needed to affect the enzyme activity in the organelles is sufficiently low for it to have a possible role in controlling the activity of this chromatin-bound enzyme.
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D002875:Chromosomes / Q000201:enzymology; D004229:Dithiothreitol / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D006367:HeLa Cells / Q000201:enzymology; D006801:Humans; D008677:Metaphase; D009244:NAD+ Nucleosidase / Q000037:antagonists & inhibitors*; D000067856:Poly(ADP-ribose) Polymerase Inhibitors; D013552:Swine; D013950:Thymus Gland / Q000201:enzymology; D015032:Zinc / Q000494:pharmacology*
D000067856:Poly(ADP-ribose) Polymerase Inhibitors; D009244:NAD+ Nucleosidase; D015032:Zinc; D004229:Dithiothreitol