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Article

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

Cell - 2 Dec 1994

Shah R, Bennett R J, West S C

Abstract excerpt

The E. coli RuvC protein resolves Holliday junctions during genetic recombination and postreplication repair. Using recombination intermediates made by RecA protein, we have identified specific "hotspots" for RuvC resolution. Characterization of these sites reveals a common tetranucleotide sequence, with the consensus 5'-A/TTT decreases G/C-3'. The correct orientation of the resolution site is required for...

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Identifiers

PMID: 8001122
DOI: 10.1016/0092-8674(94)90074-4

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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.

Related research

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Research trail→

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Genetic recombination in E. coli: RuvC protein cleaves Holliday junctions at resolution hotspots in vitro.PMID 8001122Read ↗

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

The RuvABC resolvasome.Semantic proximity Read ↗

An E. coli RuvC mutant defective in cleavage of synthetic Holliday junctions.Semantic proximity Read ↗

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

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

Sequence-specificity of Holliday junction resolution: identification of RuvC mutants defective in metal binding and target site recognition.Semantic proximity Read ↗

RuvABC is required to resolve holliday junctions that accumulate following replication on damaged templates in Escherichia coli.Semantic proximity Read ↗

Escherichia coli RuvBL268S: a mutant RuvB protein that exhibits wild-type activities in vitro but confers a UV-sensitive ruv phenotype in vivo.Semantic proximity Read ↗

Evidence that phenylalanine 69 in Escherichia coli RuvC resolvase forms a stacking interaction during binding and destabilization of a Holliday junction DNA substrate.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 ↗

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

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