Holliday junction processing in bacteria: insights from the evolutionary conservation of RuvABC, RecG, and RusA.
(1999)
Journal Article
Sharples, G., Ingleston, S., & Lloyd, R. (1999). Holliday junction processing in bacteria: insights from the evolutionary conservation of RuvABC, RecG, and RusA. Journal of Bacteriology, 181, 5543-5550
Dr Gary Sharples' Outputs (3)
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, 403-415RusA 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, 4121-4127The 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..