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

PCNA activates the Holliday junction endonuclease Hjc.

Journal of molecular biology - 1 Dec 2006

Dorazi Robert, Parker Joanne L, White Malcolm F

Abstract excerpt

The resolving enzyme Hjc, which cleaves Holliday junctions with a high degree of structural specificity, is conserved in all archaea. Like RuvC in Escherichia coli, Hjc functions in the related processes of homologous recombination and double-strand break repair. In bacteria, the RuvAB complex binds Holliday junctions and catalyses ATP-dependent branch migration, but the equivalent proteins in archaea and eukarya...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Archaeal Proteins
Share to PCNA gene

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to PIP gene

Share to Models, Molecular

Share to Mutation

Share to Proliferating Cell Nuclear Antigen

Share to Sulfolobus solfataricus

Source

Identifiers

PMID: 17011573
DOI: 10.1016/j.jmb.2006.09.011

Genes

PCNA
PIP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

PCNA activates the Holliday junction endonuclease Hjc.PMID 17011573Read ↗

The RuvABC resolvasome.Semantic proximity Read ↗

Molecular mechanisms of Holliday junction processing in Escherichia coli.Semantic proximity Read ↗

Escherichia coli RuvC protein is an endonuclease that resolves the Holliday structure.Semantic proximity Read ↗

Structure and mechanism of the RuvB Holliday junction branch migration motor.Semantic proximity Read ↗

Analysis of conserved basic residues associated with DNA binding (Arg69) and catalysis (Lys76) by the RusA holliday junction resolvase.Semantic proximity Read ↗

Mycobacterium tuberculosis RuvA induces two distinct types of structural distortions between the homologous and heterologous Holliday junctions.Semantic proximity Read ↗

Genetic recombination in E. coli: RuvC protein cleaves Holliday junctions at resolution hotspots in vitro.Semantic proximity Read ↗

The structure of Escherichia coli RusA endonuclease reveals a new Holliday junction DNA binding fold.Semantic proximity Read ↗

Genetic analysis of an archaeal Holliday junction resolvase in Escherichia coli.Semantic proximity Read ↗

Mutational analysis on structure-function relationship of a holliday junction specific endonuclease RuvC.Semantic proximity Read ↗

Hjc resolvase is a distantly related member of the type II restriction endonuclease family.Semantic proximity Read ↗

Human Mus81-Associated Endonuclease Cleaves Holliday Junctions In VitroSemantic proximity Read ↗

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