Amino acid alterations in a hydrophobic region of the TraT protein of R6-5 increase the outer membrane permeability of enteric bacteria.
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.
Sukupolvi
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S
National Public Health Institute, Helsinki, Finland.
O'Connor
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D
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
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C036297:TraT protein, E coli