Poly(ADP‐ribose) polymerase is a zinc metalloenzyme
Open Access
- 1 August 1984
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 142 (3), 503-509
- https://doi.org/10.1111/j.1432-1033.1984.tb08314.x
Abstract
Purified poly(ADP-ribose) polymerase was inhibited by 1,10-phenanthroline at pH + and competitive with DNA. The binding of DNA to the enzyme was unaffected by the inhibitor. These results suggest that a metal-containing site is involved as part of the interaction of DNA and poly(ADP-ribose) polymerase.This publication has 56 references indexed in Scilit:
- Metal content of DNA polymerase I purified from overproducing and wild type EscherichiacoliBiochemical and Biophysical Research Communications, 1983
- A fully active DNA polymerase I from Escherichia coli lacking stoichiometric zincBiochemical and Biophysical Research Communications, 1982
- Similarities in the molecular weight of poly(ADPR) polymerase from different tissues and speciesBiochemical and Biophysical Research Communications, 1981
- Purification and properties of calf thymus polyadenosine diphosphate ribose polymeraseFEBS Letters, 1977
- Yeast RNA‐polymerase B: A zinc proteinFEBS Letters, 1976
- Yeast RNA polymerase I: A eukaryotic zinc metalloenzymeBiochemical and Biophysical Research Communications, 1976
- The role of Zn(II) in transcription by T7 RNA polymeraseBiochemical and Biophysical Research Communications, 1974
- Complete dependency of poly(ADP-ribose) synthesis on DNA and its inhibition by actinomycin DBiochemical and Biophysical Research Communications, 1972
- ZINC in DNA polymerasesBiochemical and Biophysical Research Communications, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970