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

Hjc resolvase is a distantly related member of the type II restriction endonuclease family.

Nucleic acids research - 15 Nov 2000

Daiyasu H, Komori K, Sakae S, Ishino Y, Toh H

Abstract excerpt

Hjc resolvase is an archaeal enzyme involved in homologous DNA recombination at the Holliday junction intermediate. However, the structure and the catalytic mechanism of the enzyme have not yet been identified. We performed database searching using the amino acid sequence of the enzyme from Pyrococcus furiosus as a query. We detected 59 amino acid sequences showing weak but significant sequence similarity to the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Archaeal Proteins
Share to Databases, Factual

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Deoxyribonucleases, Type II Site-Specific

Share to Endodeoxyribonucleases

Share to Mutagenesis, Site-Directed

Share to Pyrococcus furiosus

Share to Sequence Homology, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 11071943
DOI: 10.1093/nar/28.22.4540
PMCID: PMC113866

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Hjc resolvase is a distantly related member of the type II restriction endonuclease family.PMID 11071943Read ↗

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

PCNA activates the Holliday junction endonuclease Hjc.Semantic proximity Read ↗

The structure of Bacillus subtilis RecU Holliday junction resolvase and its role in substrate selection and sequence-specific cleavage.Semantic proximity Read ↗

Identification of four acidic amino acids that constitute the catalytic center of the RuvC Holliday junction resolvase.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 ↗

The archaeal Hjm helicase has recQ-like functions, and may be involved in repair of stalled replication fork.Semantic proximity Read ↗

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

Two basic residues, Lys-107 and Lys-118, of RuvC resolvase are involved in critical contacts with the Holliday junction for its resolution.Semantic proximity Read ↗

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

The RecU Holliday junction resolvase acts at early stages of homologous recombination.Semantic proximity Read ↗

RecG helicase promotes DNA double-strand break repair.Semantic proximity Read ↗

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

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