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Literature summary for 3.1.21.10 extracted from

  • Zhang, J.; Mahdi, A.A.; Briggs, G.S.; Lloyd, R.G.
    Promoting and avoiding recombination: contrasting activities of the Escherichia coli RuvABC Holliday junction resolvase and RecG DNA translocase (2010), Genetics, 185, 23-37.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information RusA restores viability to polA, dam, and uvrD mutant cells lacking RuvABC Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli RusA cleaves Holliday junctions with high specificity and efficiency, and has comparatively little activity on other forms of branched DNAs unless these can adopt a four-way branched configuration mimicking a Holliday junction ?
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information RusA cleaves Holliday junctions with high specificity and efficiency, and has comparatively little activity on other forms of branched DNAs unless these can adopt a four-way branched configuration mimicking a Holliday junction Escherichia coli ?
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?

Synonyms

Synonyms Comment Organism
Holliday junction resolvase
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Escherichia coli
ruvABC
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Escherichia coli

General Information

General Information Comment Organism
malfunction strains lacking RuvABC are inviable and accumulate Holliday junctions that interfere with growth and division of the cells Escherichia coli
additional information the RegG pathway is no alternative to the RuvABC pathway for resoling Holliday junctions, since the RecG pathway is very ineffective at removing junctions. A major function of RecG is to curb potentially pathological replication initiated via PriA protein at sites remote from oriC Escherichia coli
physiological function RuvABC resolves Holliday junctions, with RuvAB driving branch migration and RuvC catalyzing junction cleavage Escherichia coli