Osmoregulation of dimer resolution at the plasmid pJHCMW1 mwr locus by Escherichia coli XerCD recombination.
Xer-mediated dimer resolution at the mwr site of plasmid pJHCMW1 is osmoregulated in Escherichia coli. Whereas under low-salt conditions, the site-specific recombination reaction is efficient, under high-salt conditions, it proceeds inefficiently. Regulation of dimer resolution is independent of H-NS and is mediated by changes in osmolarity rather than ionic effects. The low level of recombination at high salt concentrations can be overcome by high levels of PepA or by mutating the ARG box to a sequence closer to the E. coli ARG box consensus. The central region of the mwr core recombination site plays a role in regulation of site-specific recombination by the osmotic pressure of the medium.
Pham
Huong
H
Division of Molecular Genetics, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
Dery
Ken J
KJ
Sherratt
David J
DJ
Tolmasky
Marcelo E
ME
D016282:Aspartic Acid Endopeptidases / Q000494:pharmacology; D003470:Culture Media; D004254:DNA Nucleotidyltransferases / Q000235:genetics*; D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics* / Q000254:growth & development; D005656:Fungal Proteins / Q000494:pharmacology; D009154:Mutation; D009994:Osmolar Concentration; D010957:Plasmids / Q000235:genetics / Q000378:metabolism; D045522:Recombinases; D011995:Recombination, Genetic; D012965:Sodium Chloride
D003470:Culture Media; D005656:Fungal Proteins; D045522:Recombinases; D012965:Sodium Chloride; D004254:DNA Nucleotidyltransferases; C022325:aspartic proteinase A; D016282:Aspartic Acid Endopeptidases