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Article

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

Molecular microbiology - 1 Jul 2000

Michel B, Recchia G D, Penel-Colin M, Ehrlich S D, Sherratt D J

Abstract excerpt

In this work, we present evidence that indicates that RuvABC proteins resolve Holliday junctions in a way that prevents dimer formation in vivo. First, although arrested replication forks are rescued by recombinational repair in cells deficient for the Rep helicase, rep mutants do not require the XerCD proteins or the dif site for viability. This shows that the recombination events at arrested replication forks...

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Identifiers

PMID: 10931315
DOI: 10.1046/j.1365-2958.2000.01989.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Resolution of holliday junctions by RuvABC prevents dimer formation in rep mutants and UV-irradiated cells.PMID 10931315Read ↗

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