The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.

doi:10.1073/pnas.87.8.2990

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Article

The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.

Proceedings of the National Academy of Sciences of the United States of America - 1 Apr 1990

Gradwohl G, Ménissier de Murcia J M, Molinete M, Simonin F, Koken M, Hoeijmakers J H, de Murcia G

Abstract excerpt

Poly(ADP-ribose) polymerase (EC 2.4.2.30) is a zinc-binding protein that specifically binds to a DNA strand break in a zinc-dependent manner. We describe here the cloning and expression in Escherichia coli of a cDNA fragment encoding the two putative zinc fingers (FI and FII) domain of the human poly(ADP-ribose) polymerase. Using site-directed mutagenesis, we identified the amino acids involved in metal...

Topics

Amino Acid Sequence
Base Sequence
Cell Line
Cloning, Molecular
DNA, Single-Stranded
DNA-Binding Proteins
Escherichia coli
Humans
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Metalloproteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Oligonucleotide Probes

Poly(ADP-ribose) Polymerases

Protein Conformation

Substrate Specificity

Zinc

Source

Open in PubMed Open full text

Identifiers

PMID: 2109322
DOI: 10.1073/pnas.87.8.2990
PMCID: PMC53819

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2109322-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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