PMID:1409590
Citation |
Lomovskaya, O and Lewis, K (1992) Emr, an Escherichia coli locus for multidrug resistance. Proc. Natl. Acad. Sci. U.S.A. 89:8938-42 |
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Abstract |
An Escherichia coli chromosomal DNA fragment cloned on a multicopy plasmid conferred resistance to carbonylcyanide m-chlorophenylhydrazone, nalidixic acid, and a number of other toxic compounds. The sequence of the cloned emr locus located at minute 57.5 of the chromosome revealed two open reading frames, emrA and emrB. emrB encodes a highly hydrophobic 56.2-kDa peptide, with 14 potential alpha-helices to span the inner membrane. The peptide is homologous to QacA, a multidrug-resistant pump from Staphylococcus aureus, and belongs to a gene family that includes tetracycline-resistant pumps of Gram-positive bacteria and the galactose/H+ symporter of E. coli. emrA encodes a putative 42.7-kDa peptide containing a single hydrophobic domain and a large C-terminal hydrophilic domain. An active pho-fusion to the C domain suggested that EmrA is a membrane protein. Disruption of emrB significantly increased sensitivity of cells to uncouplers. The cellular content of uncoupler increased in the order: overexpressed emrB cells greater than wild type greater than emrB-. |
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Keywords |
Amino Acid Sequence; Bacterial Proteins/genetics; Base Sequence; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology; Carrier Proteins/genetics; Chromosomes, Bacterial/physiology; Drug Resistance, Microbial/genetics; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins; Genes, Bacterial; Kinetics; Membrane Proteins/genetics; Membrane Transport Proteins; Molecular Sequence Data; Multigene Family; Nalidixic Acid/pharmacology; Nitriles/pharmacology; Open Reading Frames; Polymerase Chain Reaction; Protein Biosynthesis; RNA, Messenger/genetics; Restriction Mapping; Sequence Homology, Amino Acid; Staphylococcus aureus/genetics; Tetracycline Resistance/genetics; Transcription, Genetic |
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