Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Lois M. Wentzell"'
Publikováno v:
Proceedings of the National Academy of Sciences. 99:13492-13497
In eukaryotic cells, RAD52 protein plays a central role in genetic recombination and DNA repair by ( i ) promoting the annealing of complementary single-stranded DNA and ( ii ) stimulation of the RAD51 recombinase. The single-strand annealing domain
Autor:
Anthony Maxwell, Deborah B. Zamble, Deborah Ann Miller, Lois M. Wentzell, Stephen J. Blance, Jonathan G. Heddle, Florian Hollfelder, Christopher T. Walsh
Publikováno v:
Journal of Molecular Biology. 307:1223-1234
Microcin B17 is a 3.1-kDa bactericidal peptide; the putative target of this antibiotic is DNA gyrase. Microcin B17 has no detectable effect on gyrase-catalysed DNA supercoiling or relaxation activities in vitro and is unable to stabilise DNA cleavage
Autor:
Lois M. Wentzell, Anthony Maxwell
Publikováno v:
Journal of Molecular Biology. 304:779-791
Quinolone drugs can inhibit bacterial DNA replication, via interaction with the type II topoisomerase DNA gyrase. Using a DNA template containing a preferred site for quinolone-induced gyrase cleavage, we have demonstrated that the passage of the bac
Publikováno v:
Nucleosides, Nucleotides and Nucleic Acids. 19:1249-1264
DNA gyrase supercoils DNA in bacteria. The fact that it is essential in all bacteria and absent from eukaryotes makes it an ideal drug target. We discuss the action of coumarin and quinolone drugs on gyrase. In the case of coumarins, the drugs are kn
Autor:
Stephen E. Halford, Lois M. Wentzell
Publikováno v:
Journal of Molecular Biology. 281:433-444
The SfiI endonuclease has to interact with two copies of its recognition sequence before it can cleave DNA. To demonstrate that the reaction of SfiI on a DNA with two sites involves the formation of a DNA loop, and to characterise the looping interac
Autor:
Timothy J. Nobbs, Geoffrey S. Baldwin, Lois M. Wentzell, Mark D. Szczelkun, Stephen E. Halford, I. Barry Vipond, Mark Oram, Symon G. Erskine
Publikováno v:
University of Bristol-PURE
A procedure for measuring the activities of enzymes that alter the covalent structure of DNA is described. The assay utilizes covalently closed circles of DNA as the substrate and yields quantitative data on the fraction of this DNA converted to both
Publikováno v:
Journal of molecular biology. 281(3)
A mechanism for the precise excision of DNA between two target sites was elucidated by analysing the individual steps during the reactions of the SfiI endonuclease on a plasmid with two SfiI sites. Previous studies had indicated that SfiI is a tetram
Publikováno v:
Journal of molecular biology. 248(3)
TheSfiI endonuclease cleaves DNA by a mechanism that differs from other restriction enzymes. While most restriction enzymes are dimeric proteins that interact with a single DNA site,SfiI exists in solution as a tetramer and it appears to interact wit
Publikováno v:
Biochemical Society transactions. 22(3)