Holliday Junction Binding and Resolution by the Rap Structure-specific Endonuclease of Phage λ

Sharples, Gary J.; Curtis, Fiona A.; McGlynn, Peter; Bolt, Edward L.

doi:10.1016/j.jmb.2004.05.030

Cited by 25 publications

(20 citation statements)

References 46 publications

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“…Like RusA, SLX1-SLX4 efficiently resolved the χ structure into all four duplex products ( Figure 4D). A bias towards dual incisions on strands B and D was observed for RusA in agreement with a previous report ( Figure 4D) (Sharples et al, 2004). In contrast, like RuvC (Zerbib et al, 1997), SLX1-SLX4 did not display any bias ( Figure 4D).…”

Section: Human Slx1-slx4 Has Holliday Junction Resolvase Activitysupporting

confidence: 92%

“…This much larger HJ substrate more closely resembles HJs found in vivo with a large 300 bp core of homology and long duplex arms ranging from 0.45 to 2.15 kb. It was previously used to characterize the HJ resolving activities of bacterial and phages resolvases (Sharples et al, 2004;Zerbib et al, 1997). Resolution of the χ structure yields two pairs of nicked duplex products following dual incisions on strands A and C or B and D ( Figure 4C).…”

Section: Human Slx1-slx4 Has Holliday Junction Resolvase Activitymentioning

confidence: 99%

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Human SLX4 Is a Holliday Junction Resolvase Subunit that Binds Multiple DNA Repair/Recombination Endonucleases

Fekairi¹,

Scaglione²,

Chahwan³

et al. 2009

Journal of End-to-End-testing

115

204

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SummaryStructure-specific endonucleases resolve DNA secondary structures generated during DNA repair and recombination. The yeast 5′-flap endonuclease Slx1-Slx4 has received particular attention with the finding that Slx4 has Slx1-independent key functions in genome maintenance. Although Slx1 is a highly conserved protein in eukaryotes, no orthologs of Slx4 were reported other than in fungi. Here we report the identification of Slx4 orthologs in metazoa, including fly MUS312, essential for meiotic recombination, and human BTBD12, an ATM/ATR checkpoint kinase substrate. Human SLX1-SLX4 displays robust Holliday junction resolvase activity in addition to 5′-flap endonuclease activity. Depletion of SLX1 and SLX4 results in 53BP1 foci accumulation and H2AX phosphorylation as well as cellular hypersensitivity to MMS. Furthermore, we show that SLX4 binds the XPF and MUS81 subunits of the XPF-ERCC1 and MUS81-EME1 endonucleases and is required for DNA interstrand crosslink repair. We propose that SLX4 acts as a docking platform for multiple structure-specific endonucleases.

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Section: Human Slx1-slx4 Has Holliday Junction Resolvase Activitysupporting

confidence: 92%

Section: Human Slx1-slx4 Has Holliday Junction Resolvase Activitymentioning

confidence: 99%

Human SLX4 Is a Holliday Junction Resolvase Subunit that Binds Multiple DNA Repair/Recombination Endonucleases

Fekairi¹,

Scaglione²,

Chahwan³

et al. 2009

Journal of End-to-End-testing

115

204

View full text Add to dashboard Cite

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“…and was eliminated in the dnaBgrpD55 strain. Yet the Hollifield et al (1987) identified the NinR function recJ mutation was significantly more inhibitory to NinRrap as an essential requirement for phage-plasmid codependent imm marker rescue than was the altered integration at a site of shared DNA homology ( Figure dnaB (Sharples et al 2004). We show that the nin5 deletion RecD for NinR-dependent imm rescue.…”

Section: Sieb-n-p L -Rexb-rexa and Cro-cii-o (mentioning

confidence: 53%

“…We found that 's Red or its NinR each when presented with DNA substrates containing suffifunction in the absence of the other to support imm cient homology at the crossover (Sharples et al 2004) exchange. The host requirements for the Red-or Ninand can substitute for the E. coli RuvC Holliday junction mediated imm rescue differed significantly.…”

mentioning

confidence: 79%

NinR- and Red-Mediated Phage-Prophage Marker Rescue Recombination in Escherichia coli

et al. 2005

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We examined the requirement of recombination functions for marker rescue of cryptic prophage genes within the Escherichia coli chromosome. We infected lysogenic host cells with imm434 phages and selected for recombinant imm phages that had exchanged the imm434 region of the infecting phage for the heterologous 2.6-kb imm region from the prophage. Phage-encoded activity, provided by either Red or NinR functions, was required for the substitution. Red Ϫ phages with ⌬NinR, internal NinR deletions of rap-ninH, or orf-ninC were 117-, 12-, and 5-fold reduced for imm rescue in a Rec ϩ host, suggesting the participation of several NinR activities. RecA was essential for NinR-dependent imm rescue, but had slight influence on Red-dependent rescue. The host recombination activities RecBCD, RecJ, and RecQ participated in NinR-dependent recombination while they served to inhibit Red-mediated imm rescue. The opposite effects of several host functions toward NinR-and Red-dependent imm rescue explains why the independent pathways were not additive in a Rec ϩ host and why the NinR-dependent pathway appeared dominant. We measured the influence of the host recombination functions and DnaB on the appearance of ori -dependent replication initiation and whether ori replication initiation was required for imm marker rescue.

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“…However, unlike resolvases such as RuvC from E. coli, phage T4 endonuclease VII and phage T7 endonuclease I, Rap did not promote symmetrical paired incisions in artificial Holliday junctions with fixed crossovers, or ones with limited homology (2 to 3 bp) at the core. It did, however, promote symmetrical cuts with structures containing larger regions of homology (11 to 12 bp) at the crossover point, with a preference for cutting between 5′G-C3′ dinucleotides (387). These cuts were nicks in duplex DNA, because they could be repaired by ligase.…”

Section: Other λ Functions That Influence the Mechanism Of Red Recombmentioning

confidence: 99%

λ Recombination and Recombineering

Murphy

2016

EcoSal Plus

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The bacteriophage λ Red homologous recombination system has been studied over the past 50 years as a model system to define the mechanistic details of how organisms exchange DNA segments that share extended regions of homology. The λ Red system proved useful as a system to study because recombinants could be easily generated by co-infection of genetically marked phages. What emerged from these studies was the recognition that replication of phage DNA was required for substantial Red-promoted recombination in vivo, and the critical role that double-stranded DNA ends play in allowing the Red proteins access to the phage DNA chromosomes. In the past 16 years, however, the λ Red recombination system has gained a new notoriety. When expressed independently of other λ functions, the Red system is able to promote recombination of linear DNA containing limited regions of homology (∼50 bp) with the Escherichia coli chromosome, a process known as recombineering. This review explains how the Red system works during a phage infection, and how it is utilized to make chromosomal modifications of E. coli with such efficiency that it changed the nature and number of genetic manipulations possible, leading to advances in bacterial genomics, metabolic engineering, and eukaryotic genetics.

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Holliday Junction Binding and Resolution by the Rap Structure-specific Endonuclease of Phage λ

Cited by 25 publications

References 46 publications

Human SLX4 Is a Holliday Junction Resolvase Subunit that Binds Multiple DNA Repair/Recombination Endonucleases

Human SLX4 Is a Holliday Junction Resolvase Subunit that Binds Multiple DNA Repair/Recombination Endonucleases

NinR- and Red-Mediated Phage-Prophage Marker Rescue Recombination in Escherichia coli

λ Recombination and Recombineering

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