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Article

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

Journal of molecular biology - 18 Mar 2011

Eustermann Sebastian, Videler Hortense, Yang Ji-Chun, Cole Paul T, Gruszka Dominika, Veprintsev Dmitry, Neuhaus David

Abstract excerpt

Poly(ADP-ribose)polymerase-1 (PARP-1) is a highly abundant chromatin-associated enzyme present in all higher eukaryotic cell nuclei, where it plays key roles in the maintenance of genomic integrity, chromatin remodeling and transcriptional control. It binds to DNA single- and double-strand breaks through an N-terminal region containing two zinc fingers, F1 and F2, following which its C-terminal catalytic domain...

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Identifiers

PMID: 21262234
DOI: 10.1016/j.jmb.2011.01.034
PMCID: PMC3094755

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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.

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The DNA-binding domain of human PARP-1 interacts with DNA single-strand breaks as a monomer through its second zinc finger.PMID 21262234Read ↗

Structural Basis of Detection and Signaling of DNA Single-Strand Breaks by Human PARP-1Semantic proximity Read ↗

HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation.Semantic proximity Read ↗

PARP-2 domain requirements for DNA damage-dependent activation and localization to sites of DNA damageSemantic proximity Read ↗

Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1Semantic proximity Read ↗

Updated protein domain annotation of the PARP protein family sheds new light on biological functionSemantic proximity Read ↗

Single-molecule force spectroscopy reveals binding and bridging dynamics of PARP1 and PARP2 at DNA double-strand breaksSemantic proximity Read ↗

Multifaceted Role of PARP1 in Maintaining Genome Stability Through Its Binding to Alternative DNA StructuresSemantic proximity Read ↗

Structural dynamics of DNA strand break sensing by PARP-1 at a single-molecule levelSemantic proximity Read ↗

HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histonesSemantic 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 ↗

Structural dynamics of DNA strand break sensing by PARP-1 at a single-molecule levelSemantic proximity Read ↗

A PARP2-specific active site α-helix melts to permit DNA damage-induced enzymatic activationSemantic proximity Read ↗

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