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The RdgC protein of Escherichia coli binds DNA and counters a toxic effect of RecFOR in strains lacking the replication restart protein PriA. (2003)
Journal Article
Moore, T., McGlynn, P., Ngo, H., Sharples, G., & Lloyd, R. (2003). The RdgC protein of Escherichia coli binds DNA and counters a toxic effect of RecFOR in strains lacking the replication restart protein PriA. The EMBO Journal, 22, 735-745

PriA protein provides a means to load the DnaB replicative helicase at DNA replication fork and D loop structures, and is therefore a key factor in the rescue of stalled or broken forks and subsequent replication restart. We show that the nucleoid-as... Read More about The RdgC protein of Escherichia coli binds DNA and counters a toxic effect of RecFOR in strains lacking the replication restart protein PriA..

Helicobacter pylori mutants defective in RuvC Holliday junction resolvase display reduced macrophage survival and spontaneous clearance from the murine gastric mucosa. (2003)
Journal Article
Loughlin, M., Barnard, F., Jenkins, D., Sharples, G., & Jenks, P. (2003). Helicobacter pylori mutants defective in RuvC Holliday junction resolvase display reduced macrophage survival and spontaneous clearance from the murine gastric mucosa. Infection and Immunity, 71, 2022-2031

Homologous recombination contributes to the extraordinary genetic diversity of Helicobacter pylori and may be critical for surface antigen expression and adaptation to environmental challenges within the stomach. We generated isogenic, nonpolar H. py... Read More about Helicobacter pylori mutants defective in RuvC Holliday junction resolvase display reduced macrophage survival and spontaneous clearance from the murine gastric mucosa..

A model for dsDNA translocation revealed by a structural motif common to RecG and Mfd proteins. (2003)
Journal Article
Mahdi, A., Briggs, G., Sharples, G., Wen, Q., & Lloyd, R. (2003). A model for dsDNA translocation revealed by a structural motif common to RecG and Mfd proteins. The EMBO Journal, 22, 724-734

RecG protein differs from other helicases analysed to atomic resolution in that it mediates strand separation via translocation on double-stranded (ds) rather than single-stranded (ss) DNA. We describe a highly conserved helical hairpin motif in RecG... Read More about A model for dsDNA translocation revealed by a structural motif common to RecG and Mfd proteins..

Holliday junction binding and processing by the RuvA protein of Mycoplasma pneumoniae. (2002)
Journal Article
Ingleston, S., Dickman, M., Grasby, J., Hornby, D., Sharples, G., & Lloyd, R. (2002). Holliday junction binding and processing by the RuvA protein of Mycoplasma pneumoniae. European journal of biochemistry (Internet), 269, 1525-1533

The RuvA, RuvB and RuvC proteins of Escherichia coli act together to process Holliday junctions formed during recombination and DNA repair. RuvA has a well-defined DNA binding surface that is sculptured specifically to accommodate a Holliday junction... Read More about Holliday junction binding and processing by the RuvA protein of Mycoplasma pneumoniae..

RusA proteins from the extreme thermophile Aquifex aeolicus and lactococcal phage r1t resolve Holliday junctions (2002)
Journal Article
Sharples, G., Bolt, E., & Lloyd, R. (2002). RusA proteins from the extreme thermophile Aquifex aeolicus and lactococcal phage r1t resolve Holliday junctions. Molecular Microbiology, 44(2), 549-559. https://doi.org/10.1046/j.1365-2958.2002.02916.x

The RusA protein of Escherichia coli is a DNA structure-specific endonuclease that resolves Holliday junction intermediates formed during DNA replication, recombination and repair by introducing symmetrically paired incisions 5' to CC dinucleotides.... Read More about RusA proteins from the extreme thermophile Aquifex aeolicus and lactococcal phage r1t resolve Holliday junctions.

Genetic analysis of an archaeal Holliday junction resolvase in Escherichia coli. (2001)
Journal Article
Bolt, E., Lloyd, R., & Sharples, G. (2001). Genetic analysis of an archaeal Holliday junction resolvase in Escherichia coli. Journal of Molecular Biology, 310(3), 577-589

The study of genes and proteins in heterologous model systems provides a powerful approach to the analysis of common processes in biology. Here, we show how the bacterium Escherichia coli can be exploited to analyse genetically and biochemically the... Read More about Genetic analysis of an archaeal Holliday junction resolvase in Escherichia coli..

The X philes: structure-specific endonucleases that resolve Holliday junctions. (2001)
Journal Article
Sharples, G. (2001). The X philes: structure-specific endonucleases that resolve Holliday junctions. Molecular Microbiology, 39, 823-834. https://doi.org/10.1046/j.1365-2958.2001.02284.x

Genetic recombination is a critical cellular process that promotes evolutionary diversity, facilitates DNA repair and underpins genome duplication. It entails the reciprocal exchange of single strands between homologous DNA duplexes to form a four-wa... Read More about The X philes: structure-specific endonucleases that resolve Holliday junctions..

The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome. (2000)
Journal Article
Ingleston, S., Sharples, G., & Lloyd, R. (2000). The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome. The EMBO Journal, 19, 6266-6274

Holliday junctions are four-way branched DNA structures formed during recombination, replication and repair. They are processed in Escherichia coli by the RuvA, RuvB and RuvC proteins. RuvA targets the junction and facilitates loading of RuvB helicas... Read More about The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome..

Analysis of conserved basic residues associated with DNA binding (Arg69) and catalysis (Lys76) by the RusA Holliday junction resolvase. (2000)
Journal Article
Bolt, E., Sharples, G., & Lloyd, R. (2000). Analysis of conserved basic residues associated with DNA binding (Arg69) and catalysis (Lys76) by the RusA Holliday junction resolvase. Journal of Molecular Biology, 304, 165-176

Holliday junctions are key intermediates in both homologous recombination and DNA repair, and are also formed from replication forks stalled at lesions in the template strands. Their resolution is critical for chromosome segregation and cell viabilit... Read More about Analysis of conserved basic residues associated with DNA binding (Arg69) and catalysis (Lys76) by the RusA Holliday junction resolvase..

DNA structure specificity of Rap endonuclease. (1999)
Journal Article
Sharples, G., Corbett, L., McGlynn, P., & Bolt, E. (1999). DNA structure specificity of Rap endonuclease. Nucleic Acids Research, 27, 4121-4127

The Rap protein of phage lambda is an endonuclease that nicks branched DNA structures. It has been proposed that Rap can nick D-loops formed during phage recombination to generate splice products without the need for the formation of a 4-strand (Holl... Read More about DNA structure specificity of Rap endonuclease..

Identification of three aspartic acid residues essential for catalysis by the RusA Holliday junction resolvase. (1999)
Journal Article
Bolt, E., Sharples, G., & Lloyd, R. (1999). Identification of three aspartic acid residues essential for catalysis by the RusA Holliday junction resolvase. Journal of Molecular Biology, 286, 403-415

RusA is a Holliday junction resolvase encoded by the cryptic prophage DLP12 of Escherichia coli K-12 that can be activated to promote homologous recombination and DNA repair in resolution-deficient mutants lacking the RuvABC proteins. Database search... Read More about Identification of three aspartic acid residues essential for catalysis by the RusA Holliday junction resolvase..

Structural similarities between Escherichia coli RuvA protein and other DNA-binding proteins and a mutational analysis of its binding to the Holliday junction. (1998)
Journal Article
Rafferty, J., Ingleston, S., Hargreaves, D., Artymiuk, P., Sharples, G., Lloyd, R., & Rice, D. (1998). Structural similarities between Escherichia coli RuvA protein and other DNA-binding proteins and a mutational analysis of its binding to the Holliday junction

Comparison of the structure of Escherichia coli RuvA with other proteins in the Protein Data Bank gives insights into the probable modes of association of RuvA with the Holliday junction during homologous recombination. All three domains of the RuvA... Read More about Structural similarities between Escherichia coli RuvA protein and other DNA-binding proteins and a mutational analysis of its binding to the Holliday junction..

Lambda Rap protein is a structure-specific endonuclease involved in phage recombination. (1998)
Journal Article
Sharples, G., Corbett, L., & Graham, I. (1998). Lambda Rap protein is a structure-specific endonuclease involved in phage recombination

Bacteriophage lambda encodes a number of genes involved in the recombinational repair of DNA double-strand breaks. The product of one of these genes, rap, has been purified. Truncated Rap proteins that copurify with the full-length form are derived,... Read More about Lambda Rap protein is a structure-specific endonuclease involved in phage recombination..

Sequence-specificity of Holliday junction resolution: identification of RuvC mutants defective in metal binding and target site recognition. (1998)
Journal Article
Hagan, N., Vincent, S., Ingleston, S., Sharples, G., Bennett, R., West, S., & Lloyd, R. (1998). Sequence-specificity of Holliday junction resolution: identification of RuvC mutants defective in metal binding and target site recognition. Journal of Molecular Biology, 281, 17-29

The RuvC protein of Escherichia coli resolves Holliday intermediates in recombination and DNA repair by a dual strand incision mechanism targeted to specific DNA sequences located symmetrically at the crossover. Two classes of amino acid substitution... Read More about Sequence-specificity of Holliday junction resolution: identification of RuvC mutants defective in metal binding and target site recognition..

Characterization of a thermosensitive Escherichia coli aspartyl-tRNA synthetase mutant. (1997)
Journal Article
Martin, F., Sharples, G., Lloyd, R., Eiler, S., Moras, D., Gangloff, J., & Eriani, G. (1997). Characterization of a thermosensitive Escherichia coli aspartyl-tRNA synthetase mutant. Journal of Bacteriology, 179(11), 3691-3696

The Escherichia coli tls-1 strain carrying a mutated aspS gene (coding for aspartyl-tRNA synthetase), which causes a temperature-sensitive growth phenotype, was cloned by PCR, sequenced, and shown to contain a single mutation resulting in substitutio... Read More about Characterization of a thermosensitive Escherichia coli aspartyl-tRNA synthetase mutant..

Recombination-dependent growth in exonuclease-depleted recBC sbcBC strains of Escherichia coli K-12. (1996)
Journal Article
Ryder, L., Sharples, G., & Lloyd, R. (1996). Recombination-dependent growth in exonuclease-depleted recBC sbcBC strains of Escherichia coli K-12. Genetics, 143(3), 1101-1114

Analysis of the aroLM-sbcCD interval of the Escherichia coli K-12 chromosome revealed a new gene (rdgC) encoding a function required for growth in recombination-deficient recBC sbcBC strains. Deletion of rdgC does not reduce viability, conjugational... Read More about Recombination-dependent growth in exonuclease-depleted recBC sbcBC strains of Escherichia coli K-12..

Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction. (1996)
Journal Article
Rafferty, J., Sedelnikova, S., Hargreaves, D., Artymiuk, P., Baker, P., Sharples, G., …Rice, D. (1996). Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction. Science, 274(5286), 415-421

The Escherichia coli DNA binding protein RuvA acts in concert with the helicase RuvB to drive branch migration of Holliday intermediates during recombination and DNA repair. The atomic structure of RuvA was determined at a resolution of 1.9 angstroms... Read More about Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction..

Haemophilus virulence. (1996)
Journal Article
Sharples, G. (1996). Haemophilus virulence. Microbiology, 142 ( Pt 4),