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Search Results to Kenan C Murphy PhD

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Academic Background

Ph. D. (1983) University of Maryland

Recombineering technology for gene replacement in bacterial pathogens

Identification of Drug Targets in M. tuberculosis - creating regulatable strains for use in whole cell screens with small molecules

My work invovles the use of Red recombineering technology for gene replacement in bacterial pathogens. My lab was the first to show that the lambda Red recombination system promotes gene replacement of electroporated linear DNA substrates into the Escherichia coliK-12 chromosome at a very high efficiency (Murphy, 1998). The system is also useful in pathogenic species of E. coli (Murphy & Campellone, 2003). Work continues to improve recombinering technology in pathogens such as Pseudomonas aeruginosa and Mycobacterium tuberculosis by expression of Red-lke recombination systems from phage known to infect these hosts.

 

My lab is also interested in the mechnaism of the bacteriophage lambda Red recombination system. The system consist of two proteins, the ssDNA annealing Bet protein and the 5’-3’ dsDNA lambda exonuclease. These two proteins form a complex in vitro, and are thought to interact with each other in vivo. We have isolated various mutants of Bet that are deficient for both recombination and recombineering, and some that are deficient for one but not the other.   

 

 

Proposed mechanism of Red Recombineering

Lambda Exo's 5' exonuclease activity (red trapezoid)) generates ssDNA, which serves as a substrate for lambda Bet (blue oligomeric ring) to bind and promote annealing to ssDNA in the lagging strand of a replication fork. This structure is stabilized by the lambda Beta protein, unitl another fork comes by and generates both a wild type and a recombinant chromosome.

replication Kenan Murphy figure page


One or more keywords matched the following items that are connected to Murphy, Kenan

Item TypeName
Academic Article PCR-mediated gene replacement in Escherichia coli.
Academic Article Mutational analysis of the MutH protein from Escherichia coli.
Academic Article Dam methyltransferase is required for stable lysogeny of the Shiga toxin (Stx2)-encoding bacteriophage 933W of enterohemorrhagic Escherichia coli O157:H7.
Academic Article Transcriptional regulators of the GAD acid stress island are carried by effector protein-encoding prophages and indirectly control type III secretion in enterohemorrhagic Escherichia coli O157:H7.
Academic Article Structural/functional analysis of the human OXR1 protein: identification of exon 8 as the anti-oxidant encoding function.
Academic Article Lambda Red-mediated recombinogenic engineering of enterohemorrhagic and enteropathogenic E. coli.
Academic Article Increased adherence and actin pedestal formation by dam-deficient enterohaemorrhagic Escherichia coli O157:H7.
Academic Article The lambda Gam protein inhibits RecBCD binding to dsDNA ends.
Academic Article Rapid allelic exchange in enterohemorrhagic Escherichia coli (EHEC) and other E. coli using lambda red recombination.
Academic Article Targeted chromosomal gene knockout using PCR fragments.
Academic Article Enhanced Actin Pedestal Formation by Enterohemorrhagic Escherichia coli O157:H7 Adapted to the Mammalian Host.
Academic Article Identification of a novel prophage regulator in Escherichia coli controlling the expression of type III secretion.
Academic Article High incidence of multiple antibiotic resistant cells in cultures of in enterohemorrhagic Escherichia coli O157:H7.
Concept Escherichia coli Infections
Concept Escherichia coli
Concept Escherichia coli O157
Concept Escherichia coli Proteins
Concept Enterohemorrhagic Escherichia coli
Academic Article Use of bacteriophage lambda recombination functions to promote gene replacement in Escherichia coli.
Academic Article Biochemical characterization of P22 phage-modified Escherichia coli RecBCD enzyme.
Academic Article Properties of Escherichia coli expressing bacteriophage P22 Abc (anti-RecBCD) proteins, including inhibition of Chi activity.
Academic Article Lambda Gam protein inhibits the helicase and chi-stimulated recombination activities of Escherichia coli RecBCD enzyme.

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  • Escherichia coli