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Article

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

The Journal of biological chemistry - 29 Sept 2006

Donaldson Janet R, Courcelle Charmain T, Courcelle Justin

Abstract excerpt

RuvABC is a complex that promotes branch migration and resolution of Holliday junctions. Although ruv mutants are hypersensitive to UV irradiation, the molecular event(s) that necessitate RuvABC processing in vivo are not known. Here, we used a combination of two-dimensional gel analysis and electron microscopy to reveal that although ruvAB and ruvC mutants are able to resume replication following arrest at...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Electrophoresis, Gel, Two-Dimensional

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Source

Identifiers

PMID: 16895921
DOI: 10.1074/jbc.M603933200

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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.

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RuvABC is required to resolve holliday junctions that accumulate following replication on damaged templates in Escherichia coli.PMID 16895921Read ↗

ruvA Mutants that resolve Holliday junctions but do not reverse replication forks.Semantic proximity Read ↗

RuvAB acts at arrested replication forks.Semantic proximity Read ↗

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

Formation of a stable RuvA protein double tetramer is required for efficient branch migration in vitro and for replication fork reversal in vivo.Semantic proximity Read ↗

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

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

RuvAB is essential for replication forks reversal in certain replication mutants.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 ↗

Resolution of holliday junctions by RuvABC prevents dimer formation in rep mutants and UV-irradiated cells.Semantic proximity Read ↗

The RuvABC resolvasome.Semantic proximity Read ↗

Abortive recombination in Escherichia coli ruv mutants blocks chromosome partitioning.Semantic proximity Read ↗

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