title: Amino acid alterations in a hydrophobic region of the TraT protein of R6-5 increase the outer membrane permeability of enteric bacteria.
abstract: Two insertion mutations, each introducing a new negatively charged amino acid residue into a hydrophobic region of the TraT protein coded by the F-like plasmid R6-5 caused significant alterations in outer membrane permeability of Escherichia coli and Salmonella typhimurium, so that strains carrying plasmids with either of these mutations became sensitive to hydrophobic antibiotics.
authors.affiliation: National Public Health Institute, Helsinki, Finland.
authors.forename: S
authors.initials: S
authors.lastname: Sukupolvi
authors.forename: D
authors.initials: D
authors.lastname: O'Connor
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D002463:Cell Membrane Permeability; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D009154:Mutation; D010957:Plasmids; D012486:Salmonella typhimurium / Q000235:genetics* / Q000378:metabolism
chemical_list: D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C036297:TraT protein, E coli