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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..

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..

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..

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..

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

Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82. (1996)
Journal Article
Mahdi, A., Sharples, G., Mandal, T., & Lloyd, R. (1996). Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82

The RusA protein of Escherichia coli is an endonuclease that can resolve Holliday intermediates and correct the defects in genetic recombination and DNA repair associated with inactivation of RuvAB or RuvC. The structure of the rusA gene, its organis... Read More about Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82..

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..

The mmsA locus of Streptococcus pneumoniae encodes a RecG-like protein involved in DNA repair and in three-strand recombination. (1996)
Journal Article
Martin, B., Sharples, G., Humbert, O., Lloyd, R., & Claverys, J. (1996). The mmsA locus of Streptococcus pneumoniae encodes a RecG-like protein involved in DNA repair and in three-strand recombination. Molecular Microbiology, 19(5), 1035-1045

We describe the characterization of a mutant strain of Streptococcus pneumoniae previously isolated on the basis of its sensitivity to Methyl Methane Sulphonate (MMS). The mutant strain also exhibited increased sensitivity to UV light and to X-rays,... Read More about The mmsA locus of Streptococcus pneumoniae encodes a RecG-like protein involved in DNA repair and in three-strand recombination..

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..

Cloning, overexpression, purification, and characterization of the Escherichia coli RuvC Holliday junction resolvase. (1994)
Journal Article
Dunderdale, H., Sharples, G., Lloyd, R., & West, S. (1994). Cloning, overexpression, purification, and characterization of the Escherichia coli RuvC Holliday junction resolvase. Journal of Biological Chemistry, 269(7), 5187-5194

The ruvC gene has been cloned into the plasmid pT7-7 under the control of the T7 phi 10 promoter. Following induction with isopropyl-1-thio-beta-D-galactopyranoside, the 19-kDa RuvC protein was overexpressed to 20-30% of total cell protein. RuvC has... Read More about Cloning, overexpression, purification, and characterization of the Escherichia coli RuvC Holliday junction resolvase..

A mutation in helicase motif III of E. coli RecG protein abolishes branch migration of Holliday junctions. (1994)
Journal Article
Sharples, G., Whitby, M., Ryder, L., & Lloyd, R. (1994). A mutation in helicase motif III of E. coli RecG protein abolishes branch migration of Holliday junctions. Nucleic Acids Research, 22(3), 308-313

The RecG protein of Escherichia coli catalyses branch migration of Holliday junctions made by RecA and dissociates synthetic X junctions into duplex products in reactions that require hydrolysis of ATP. To investigate the mode of action of this enzym... Read More about A mutation in helicase motif III of E. coli RecG protein abolishes branch migration of Holliday junctions..

Processing of intermediates in recombination and DNA repair: identification of a new endonuclease that specifically cleaves Holliday junctions. (1994)
Journal Article
Sharples, G., Chan, S., Mahdi, A., Whitby, M., & Lloyd, R. (1994). Processing of intermediates in recombination and DNA repair: identification of a new endonuclease that specifically cleaves Holliday junctions. The EMBO Journal, 13(24), 6133-6142

The formation and subsequent resolution of Holliday junctions are critical stages in recombination. We describe a new Escherichia coli endonuclease that resolves Holliday intermediates by junction cleavage. The 14 kDa Rus protein binds DNA containing... Read More about Processing of intermediates in recombination and DNA repair: identification of a new endonuclease that specifically cleaves Holliday junctions..

Dissociation of synthetic Holliday junctions by E. coli RecG protein. (1993)
Journal Article
Lloyd, R., & Sharples, G. (1993). Dissociation of synthetic Holliday junctions by E. coli RecG protein. The EMBO Journal, 12(1), 17-22

The RecG protein of Escherichia coli is needed for normal levels of recombination and for repair of DNA damaged by ultraviolet light, mitomycin C and ionizing radiation. The true extent of its involvement in these processes is masked to a large degre... Read More about Dissociation of synthetic Holliday junctions by E. coli RecG protein..