Recombinant E. coli RuvC protein (Active)
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(4 Publications)
Recombinant E. coli RuvC protein (Active) is a Escherichia coli K-12 Full Length protein, expressed in Escherichia coli, with >90%, suitable for ELISA, WB, FuncS, SDS-PAGE.
View Alternative Names
b1863, JW1852, ruvC, Crossover junction endodeoxyribonuclease RuvC, Holliday junction endonuclease RuvC, Holliday junction nuclease RuvC, Holliday junction resolvase RuvC
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant E. coli RuvC protein (Active) (AB63828)
SDS-PAGE analysis of Recombinant E. coli RuvC protein (ab63828).
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
RuvC ensures proper segregation of homologous chromosomes by processing DNA during cell division. It operates as a part of the RuvABC complex which consists of the RuvA and RuvB proteins in addition to RuvC. RuvA binds to the Holliday junctions and recruits RuvB forming a branch migration motor. RuvC then cleaves the junctions resolving them. This activity plays a major role in maintaining genetic stability by enabling the accurate exchange of genetic material.
Pathways
RuvC contributes significantly to homologous recombination and DNA repair mechanisms. It participates within the homologous recombination repair pathway intertwining with proteins such as RecA which facilitates the alignment of homologous DNA sequences and RecBCD a helicase/nuclease involved in processing DNA double-strand breaks. RuvC acts after RecA-mediated strand invasion to resolve recombination intermediates.
Specifications
Form
Liquid
General info
Function
The RuvA-RuvB-RuvC complex processes Holliday junctions during genetic recombination and DNA repair (PubMed : 6374379). Endonuclease that resolves Holliday junction (HJ) intermediates. Cleaves cruciform DNA by making single-stranded nicks across the junction at symmetrical positions within the homologous arms, leaving a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction (PubMed : 10471285, PubMed : 1661673, PubMed : 1758493, PubMed : 1829835, PubMed : 36000732, PubMed : 8001122, PubMed : 8106500, PubMed : 8195150, PubMed : 9000618, PubMed : 9135161, PubMed : 9160752). The consensus cleavage sequence is 5'-(A/T)TT(C>G/A)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange, although there is some flexibility in the position cleaved (PubMed : 10471285, PubMed : 8001122, PubMed : 8195150, PubMed : 9135161). The cleavage reactions can be uncoupled; incision requires the presence of two consensus cleavage sequences, although they do not have to be identical (PubMed : 9135161). The presence of a 5'-phosphate in a half-cut site accelerates cleavage of the second site, ensuring the second cleavage occurs within the lifetime of a single RuvC-HJ complex (PubMed : 19399178). Binds to cruciform DNA in a sequence non-specific manner (PubMed : 10471285, PubMed : 8106500, PubMed : 8195150).. An in vitro resolvase system that forms and processes HJ has been reconstituted with DNA substrates, RuvA, RuvB and RuvC. RuvA-RuvB increases the rate of strand exchange (branch migration), dissociates the RecA filament and allows RuvC to cleave in both orientations at the cruciform junction (PubMed : 10421637, PubMed : 9160752). HJ-RuvA-RuvB-RuvC complexes resolve Holliday junctions and also undergo branch migration, providing evidence for a coupled branch migration/HJ resolution reaction (PubMed : 10421637).
Sequence similarities
Belongs to the RuvC family.
Target data
Publications (4)
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Nucleic acids research 51:9144-9165 PubMed37526271
2023
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Nucleic acids research 49:2803-2815 PubMed33619520
2021
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Molecular cell 69:9-23.e6 PubMed29290614
2018
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Nature communications 5:5652 PubMed25466415
2014
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