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Mutational analysis on structure-function relationship of a holliday junction specific endonuclease RuvC.

Genes to cells : devoted to molecular & cellular mechanisms - 1 Sept 1998

Ichiyanagi K, Iwasaki H, Hishida T, Shinagawa H

Abstract excerpt

BACKGROUND: Escherichia coli RuvC protein is a specific endonuclease that resolves Holliday junctions during homologous recombination. For junction resolution, RuvC undergoes distinct steps such as dimerization, junction-specific binding and endonucleolytic cleavage. The crystal structure of RuvC has been revealed. RESULTS: To identify functionally important residues, we isolated a large number of mutant ruvC...

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PMID: 9813108
DOI: 10.1046/j.1365-2443.1998.00213.x

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Mutational analysis on structure-function relationship of a holliday junction specific endonuclease RuvC.PMID 9813108Read ↗

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

Analysis of conserved basic residues associated with DNA binding (Arg69) and catalysis (Lys76) by the RusA holliday junction resolvase.Semantic proximity Read ↗

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Modulation of RuvB function by the mobile domain III of the Holliday junction recognition protein RuvA.Semantic proximity Read ↗

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