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Article

Escherichia coli RuvC protein is an endonuclease that resolves the Holliday structure.

The EMBO journal - 1 Dec 1991

Iwasaki H, Takahagi M, Shiba T, Nakata A, Shinagawa H

Abstract excerpt

Genetic evidence suggests that the Escherichia coli ruvC gene is involved in DNA repair and in the late step of RecE and RecF pathway recombination. To study the biochemical properties of RuvC protein, we overproduced and highly purified the protein. By employing model substrates, we examined the possibility that RuvC protein is an endonuclease that resolves the Holliday structure, an intermediate in genetic...

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Identifiers

PMID: 1661673
DOI: 10.1002/j.1460-2075.1991.tb05016.x
PMCID: PMC453191

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Escherichia coli RuvC protein is an endonuclease that resolves the Holliday structure.PMID 1661673Read ↗

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The RuvABC resolvasome.Semantic proximity Read ↗

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

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

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Conjugational recombination in resolvase-deficient ruvC mutants of Escherichia coli K-12 depends on recG.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 ↗

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