Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Base Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell Line

Share to Cloning, Molecular

Share to DNA-Binding Proteins

Share to Escherichia coli

Share to Molecular Sequence Data

Share to Mutation

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 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.PMID 2109322Read ↗

Zinc Finger Nucleases as tools to understand and treat human diseasesSemantic proximity Read ↗

Binding of TFIIB to RNA polymerase II: Mapping the binding site for the TFIIB zinc ribbon domain within the preinitiation complex.Semantic proximity Read ↗

The DNA-binding domain of human PARP-1 interacts with DNA single-strand breaks as a monomer through its second zinc finger.Semantic proximity Read ↗

Overproduction of the poly(ADP-ribose) polymerase DNA-binding domain blocks alkylation-induced DNA repair synthesis in mammalian cells.Semantic proximity Read ↗

The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction.Semantic proximity Read ↗

Targeting of histone tails by poly(ADP-ribose).Semantic proximity Read ↗

Dual role for Zn2+ in maintaining structural integrity and inducing DNA sequence specificity in a promiscuous endonuclease.Semantic proximity Read ↗

A nonconserved surface of the TFIIB zinc ribbon domain plays a direct role in RNA polymerase II recruitment.Semantic proximity Read ↗

Zinc finger phage: affinity selection of fingers with new DNA-binding specificities.Semantic proximity Read ↗

A zinc-binding site in the largest subunit of DNA-dependent RNA polymerase is involved in enzyme assembly.Semantic proximity Read ↗

A conserved zinc binding domain in the largest subunit of DNA-dependent RNA polymerase modulates intrinsic transcription termination and antitermination but does not stabilize the elongation complex.Semantic proximity Read ↗

Interaction of the TFIIB zinc ribbon with RNA polymerase II.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.