Identification and molecular characterization of an efflux system involved in Pseudomonas putida S12 multidrug resistance
Article Abstract:
An efflux pump, ArpABC, involved in Pseudomonas putida S12 multidrug resistance has been studied. The arpABC operon is involved in the active efflux of various antibiotics. ArpABC does not contribute to organic solvent tolerance in P. putida 512. The deduced amino acid sequences encoded by the three involved genes show striking resemblance to proteins of the resistance/nodulation/cell division family involved in both organic solvent and multiple drug efflux. ArpABC has been shown to be highly homologous to the MepABC and TtgABC efflux systems for organic solvents and various antibiotics.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2001
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Complementation of Xanthobacter Py2 mutants defective in epoxyalkane degradation, and expression and nucleotide sequence of the complementing DNA fragment
Article Abstract:
Standard techniques help isolate and characterize three Xanthobacter Py2 mutants, M3, M8 and M10, defective in epoxyalkane degradation. The mutation in M10 and M8 is complemented by three cosmids, while they fail to complement in mutant M3. Expression of the cosmid pEP9 in Xanthobacter autotrophicus GJ10 induces epoxyalkane-degrading activity. Complementation in mutant M10 requires a 4.8 Kb EcoRI-HindIII fragment and sequence analysis reveals the presence of four different open reading frames in the fragment.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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Porin alteration and active efflux: two in vivo drug resistance strategies used by Enterobacter aerogenes
Article Abstract:
Research was conducted to examine the two drug resistance techniques used by Enterobacter aerogenes, namely, porin alteration and active efflux. Modified envelope permeability was tested in 27 E aerogenes isolates which harbor high cross-resistance against a number of standard antibiotics. Results indicated that the loss of entry channels is a bacterial response against cefepime and other new cephalosporins with configurations well-adapted to bacterial porins and stability to enzymic attack.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
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