ruvA Antibody, Biotin conjugated

1. Regression of replication forks stalled by leading-strand template damage: both RecG and RuvAB catalyze regression, but RuvC cleaves the holliday junctions formed by RecG preferentially. PMID: 25138216
2. These results suggest that RecQ acts upstream of RuvABC, RecG and XerC proteins, a finding that is compatible with its primary role in initiation of the RecF recombination pathway. PMID: 24036154
3. RNA polymerase mutations reduce the synergism between priB and ruvABC. PMID: 22957744
4. DNA fragmentation absolutely depends on both RecA-catalyzed homologous strand exchange and RuvABC-catalyzed Holliday junction resolution PMID: 22194615
5. Role in converting the initial single-strand DNA-protein cleavage complex into a double-strand break prior to repair by homologous recombination. PMID: 20601468
6. Study hypothesized that RuvAB catalyzes replication fork reversal in order to produce SOS(Con) expression. PMID: 20304994
7. RuvA octamerization is essential for the full biological activity of RuvABC. PMID: 15556943
8. RuvA is less mobile at a heterologous junction compared to a homologous junction, as two opposing DnaB pumps are required to mobilize RuvA over heterologous DNA. PMID: 16324713
9. RuvABC is required to resolve junctions that arise during the repair of a subset of nonarresting lesions after replication has passed through the template PMID: 16895921
10. The authors present here the isolation and characterization of ruvA and ruvB single mutants that are impaired for replication fork reversal at forks arrested by the inactivation of polymerase III, while they remain capable of homologous recombination. PMID: 18942176

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KEGG: ecj:JW1850

STRING: 316385.ECDH10B_2002