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Article

An E. coli RuvC mutant defective in cleavage of synthetic Holliday junctions.

Nucleic acids research - 25 Jul 1993

Sharples G J, Lloyd R G

Abstract excerpt

Escherichia coli RuvC protein is a specific endonuclease that resolves recombination intermediates into viable products. The structural features needed for RuvC activity were investigated by sequencing three ruvC mutations and relating the base pair changes identified to the activity of the mutant proteins. Each of the three mutations is a single base-pair substitution. ruvC51 converts glycine-15 to an aspartic...

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Identifiers

PMID: 8393986
DOI: 10.1093/nar/21.15.3359
PMCID: PMC331431

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An E. coli RuvC mutant defective in cleavage of synthetic Holliday junctions.PMID 8393986Read ↗

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

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

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

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

Identification of four acidic amino acids that constitute the catalytic center of the RuvC 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 ↗

The RuvABC resolvasome.Semantic proximity Read ↗

Molecular mechanisms of Holliday junction processing 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 ↗

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 ↗

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

Genetic and biochemical characterization of a novel umuD mutation: insights into a mechanism for UmuD self-cleavage.Semantic proximity Read ↗

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