Recombinant Escherichia coli Holliday junction ATP-dependent DNA helicase RuvA (ruvA), Escherichia coli (strain K12), E.coli, N-terminal 6xHis-SUMO-tagged, 38.1kDa, purity >90% as determined by SDS-PAGE.

Recombinant Escherichia coli Holliday junction ATP-dependent DNA helicase RuvA (ruvA)

Recombinant Escherichia coli Holliday junction ATP-dependent DNA helicase RuvA (ruvA) — An in vitro resolvase system that forms and processes HJ has been reconstituted with DNA substrates, RuvA, RuvB and RuvC. Purity >90%.

SKU: BCRECP-004305 Category:
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Product Specifications

Product SkuBCRECP-004305
Product DescriptionRecombinant Escherichia coli Holliday junction ATP-dependent DNA helicase RuvA (ruvA) Protein is expressed from E.coli with N-terminal 6xHis-SUMO-tagged. It contains 1-203aa. [Accession | P0A809].
Uniprot No.P0A809
Gene NamesruvA
PurityGreater than 90% as determined by SDS-PAGE.
Expression SystemE.coli
Expression Region1-203aa
SpeciesEscherichia coli (strain K12)
Tag InfoN-terminal 6xHis-SUMO-tagged
Molecular weight38.1kDa
ActivityPlease contact us to obtain bioactivity data.
BufferIf the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Research AreasOthers

Function

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. HJ-RuvA-RuvB-RuvC complexes resolve Holliday junctions and also undergo branch migration, providing evidence for a coupled branch migration/HJ resolution reaction.

Biological Context

Subcellular Location: Cytoplasm

Product Specifications

Recombinant Escherichia coli Holliday junction ATP-dependent DNA helicase RuvA (ruvA) is a recombinant protein from Escherichia coli (strain K12), expressed in E.coli, covering amino acids 1-203aa, with N-terminal 6xHis-SUMO-tagged tag, molecular weight 38.1kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

Recommended applications depend on the target, product format, and product-specific validation data. Refer to the product datasheet or Certificate of Analysis (CoA), or contact BioCrest Sci for application guidance.

Biological Activity: Please contact us to obtain bioactivity data.

Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shipping & Lead Time: Availability, shipping conditions, and estimated lead time are confirmed in the formal quotation or order confirmation based on the product format, destination, and order requirements.

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Protein Biology

Function

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)

Subcellular Location

Cytoplasm

Subunit

Homotetramer (PubMed:10772859, PubMed:10890893, PubMed:1435721, PubMed:7885479, PubMed:8832889, PubMed:9493263, PubMed:9628481). Forms a stable RuvA-RuvB-Holliday junction (HJ) complex in the presence of non-hydrolyzable (d)NTPs; in the presence of hydrolyzable (d)NTPs branch migration occurs (PubMed:7885479, PubMed:8393934). In electron microscopic images the complex is formed by 2 oppositely facing RuvB hexamers sandwiching possibly 2 RuvA tetramers at cruciform DNA structures (PubMed:7885479, PubMed:9047358). In E.coli X-ray structures only 1 RuvA tetramer binds to HJ (complex I); however in M.leprae and T.thermophilus, 2 RuvA tetramers bind the HJ (complex II) (PubMed:10890893, PubMed:9628481). Mutagenesis experiments that prevent RuvA complex II formation on HJ DNA have impaired function, suggesting both complex I and complex II are physiologically important. Y-junction resolution is normal in these mutants, further suggesting each RuvA tetramer supports the activity of one RuvB hexamer. Mutants that don't make complex II are impaired in replication fork reversal (RFR), suggesting complex II exists in vivo (PubMed:15556943, PubMed:21531731). Forms a complex with RuvB without DNA; RuvA-RuvC complexes were not detected in the absence of DNA (PubMed:9160752). Can form complexes with RuvC and HJ DNA which inhibits RuvC activity (PubMed:15556943, PubMed:21531731, PubMed:9000618, PubMed:9637927). In the presence of HJ DNA a DNA-RuvA-RuvB-RuvC complex forms with 2 rings of RuvB that resolves upon addition of ATP. Upon HJ resolution the protein complex dissociates from DNA (PubMed:10421637, PubMed:9637927)

Gene: ruvA  |  Organism: Escherichia coli (strain K12)
Key Publications

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