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Dr Gary Sharples' Outputs (82)

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..

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

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..

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..

An E. coli RuvC mutant defective in cleavage of synthetic Holliday junctions. (1993)
Journal Article
Sharples, G., & Lloyd, R. (1993). An E. coli RuvC mutant defective in cleavage of synthetic Holliday junctions. Nucleic Acids Research, 21(15), 3359-3364

Escherichia coli RuvC protein is a specific endonuclease that resolves recombination intermediates into viable products. The structural features needed for RuvC activity were investigated by sequencing three ruvC mutations and relating the base pair... Read More about An E. coli RuvC mutant defective in cleavage of synthetic Holliday junctions..

Processing of recombination intermediates by the RecG and RuvAB proteins of Escherichia coli. (1993)
Journal Article
Lloyd, R., & Sharples, G. (1993). Processing of recombination intermediates by the RecG and RuvAB proteins of Escherichia coli. Nucleic Acids Research, 21(8), 1719-1725

The RuvAB, RuvC and RecG proteins of Escherichia coli process intermediates in recombination and DNA repair into mature products. RuvAB and RecG catalyse branch migration of Holliday junctions, while RuvC resolves these structures by nuclease cleavag... Read More about Processing of recombination intermediates by the RecG and RuvAB proteins of Escherichia coli..

Resolution of Holliday intermediates in recombination and DNA repair: indirect suppression of ruvA, ruvB, and ruvC mutations. (1993)
Journal Article
Mandal, T., Mahdi, A., Sharples, G., & Lloyd, R. (1993). Resolution of Holliday intermediates in recombination and DNA repair: indirect suppression of ruvA, ruvB, and ruvC mutations. Journal of Bacteriology, 175(14), 4325-4334

The ruvA, ruvB, and ruvC genes of Escherichia coli provide activities that catalyze branch migration and resolution of Holliday junction intermediates in recombination. Mutation of any one of these genes interferes with recombination and reduces the... Read More about Resolution of Holliday intermediates in recombination and DNA repair: indirect suppression of ruvA, ruvB, and ruvC mutations..

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..

Genetic analysis of recombination in prokaryotes. (1992)
Journal Article
Lloyd, R., & Sharples, G. (1992). Genetic analysis of recombination in prokaryotes. Current Opinion in Genetics and Development, 2(5), 683-690

Bacteria provide a simple system for the genetic analysis of homologous recombination. More than twenty genes have been identified in Escherichia coli. The enzymatic activities associated with the products of many of these genes have been revealed by... Read More about Genetic analysis of recombination in prokaryotes..

Resolution of Holliday junctions in Escherichia coli: identification of the ruvC gene product as a 19-kilodalton protein. (1991)
Journal Article
Sharples, G., & Lloyd, R. (1991). Resolution of Holliday junctions in Escherichia coli: identification of the ruvC gene product as a 19-kilodalton protein. Journal of Bacteriology, 173(23), 7711-7715

The ruvC gene of Escherichia coli specifies a nuclease that resolves Holliday junction intermediates in genetic recombination (B. Connolly, C.A. Parsons, F.E. Benson, H.J. Dunderdale, G.J. Sharples, R.G. Lloyd, and S.C. West, Proc. Natl. Acad, Sci. U... Read More about Resolution of Holliday junctions in Escherichia coli: identification of the ruvC gene product as a 19-kilodalton protein..

Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins. (1991)
Journal Article
Dunderdale, H., Benson, F., Parsons, C., Sharples, G., Lloyd, R., & West, S. (1991). Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins. Nature, 354(6354), 506-510

The recombination of DNA molecules has been reconstituted in vitro using two purified enzymes from Escherichia coli. RecA protein catalyses homologous pairing and strand exchange reactions to form intermediate DNA structures that are acted upon by Ru... Read More about Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins..

Location of a mutation in the aspartyl-tRNA synthetase gene of Escherichia coli K12. (1991)
Journal Article
Sharples, G., & Lloyd, R. (1991). Location of a mutation in the aspartyl-tRNA synthetase gene of Escherichia coli K12. Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis, 264(3), 93-96

A mutation (tls-1) that confers a temperature-sensitive growth phenotype in Escherichia coli was shown by DNA cloning and sequencing to be an allele of aspS, the gene for aspartyl-tRNA synthetase. The mutation, which lies near minute 41 on the geneti... Read More about Location of a mutation in the aspartyl-tRNA synthetase gene of Escherichia coli K12..

Resolution of Holliday junctions in vitro requires the Escherichia coli ruvC gene product. (1991)
Journal Article
Connolly, B., Parsons, C., Benson, F., Dunderdale, H., Sharples, G., Lloyd, R., & West, S. (1991). Resolution of Holliday junctions in vitro requires the Escherichia coli ruvC gene product. Proceedings of the National Academy of Sciences, 88(14), 6063-6067

In previous studies, Holliday junctions generated during RecA-mediated strand-exchange reactions were resolved by fractionated Escherichia coli extracts. We now report the specific binding and cleavage of synthetic Holliday junctions (50 base pairs l... Read More about Resolution of Holliday junctions in vitro requires the Escherichia coli ruvC gene product..

Molecular organization and nucleotide sequence of the recG locus of Escherichia coli K-12. (1991)
Journal Article
Lloyd, R., & Sharples, G. (1991). Molecular organization and nucleotide sequence of the recG locus of Escherichia coli K-12. Journal of Bacteriology, 173(21), 6837-6843

The nucleotide sequence of the Escherichia coli K-12 recG gene was determined. recG was identified as an open reading frame located between the spoT operon and the convergent gltS gene. It encodes a polypeptide of 693 amino acids which was identified... Read More about Molecular organization and nucleotide sequence of the recG locus of Escherichia coli K-12..

A novel repeated DNA sequence located in the intergenic regions of bacterial chromosomes. (1990)
Journal Article
Sharples, G., & Lloyd, R. (1990). A novel repeated DNA sequence located in the intergenic regions of bacterial chromosomes. Nucleic Acids Research, 18(22), 6503-6508

We report the discovery of a novel group of highly conserved DNA sequences located within the intergenic regions of the chromosomes of Escherichia coli, Salmonella typhimurium and other bacteria. These intergenic repeat units (IRUs) are 124-127 nucle... Read More about A novel repeated DNA sequence located in the intergenic regions of bacterial chromosomes..