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Article

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

Journal of molecular biology - 7 Aug 1998

Hagan N F, Vincent S D, Ingleston S M, Sharples G J, Bennett R J, West S C, Lloyd R G

Abstract excerpt

The RuvC protein of Escherichia coli resolves Holliday intermediates in recombination and DNA repair by a dual strand incision mechanism targeted to specific DNA sequences located symmetrically at the crossover. Two classes of amino acid substitutions are described that provide new insights into the sequence-specificity of the resolution reaction. The first includes D7N and G14S, which modify or eliminate metal...

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Identifiers

PMID: 9680472
DOI: 10.1006/jmbi.1998.1934

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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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Sequence-specificity of Holliday junction resolution: identification of RuvC mutants defective in metal binding and target site recognition.PMID 9680472Read ↗

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

An E. coli RuvC mutant defective in cleavage of synthetic Holliday junctions.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 RuvC protein is an endonuclease that resolves the Holliday structure.Semantic proximity Read ↗

The RuvABC resolvasome.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 ↗

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 ↗

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

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

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