Phenotypic Association between the Outer Membrane Protein OmpW and the Small Multi-Drug Resistance Protein EmrE in Escherichia coli
Date
2014-09-02
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Abstract
In Escherichia coli, the small multidrug resistance (SMR) transporter protein EmrE confers host resistance to a broad range of toxic quaternary cationic compounds (QCCs) via proton motive force in the cytoplasmic membrane. Biologically produced QCCs also act as EmrE osmoprotectant substrates within the cell and participate in host pH regulation and osmotic tolerance. Although E. coli EmrE is one of the most well-characterized SMR members, it is unclear how the substrates that it transports into the periplasmic space escape across the outer membrane (OM) in Gram-negative bacteria. We tested the hypothesis that E. coli EmrE relies on an unidentified OM protein (OMP) to complete the extracellular release of its QCC. By conducting pH-based phenotypic growth screens, complementation and methyl viologen (MV) resistance assays, we have confirmed that EmrE relies on the presence of an OMP, specifically OmpW, to complete its extracellular substrate efflux across the OM.
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Microbiology
Citation
Beketskaia, M. (2014). Phenotypic Association between the Outer Membrane Protein OmpW and the Small Multi-Drug Resistance Protein EmrE in Escherichia coli (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/27333