Outer membrane protein OmpW participates with small multidrug resistance protein member EmrE in quaternary cationic compound efflux.

ABSTRACT: In Escherichia coli, the small multidrug resistance (SMR) transporter protein EmrE confers host resistance to a broad range of toxic quaternary cation compounds (QCC) via proton motive force in the plasma membrane. Biologically produced QCC 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 it transports into the periplasm 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. Eleven OMP candidates were screened using an alkaline phenotypic growth assay to identify OMP invol

SUBMITTER: Beketskaia MS 

PROVIDER: S-EPMC4011002 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature