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Characterization of the traT gene and mutants that increase outer membrane permeability from the Salmonella typhimurium virulence plasmid
Author(s) -
Sukupolvi S.,
Vuorio R.,
Qi S.Y.,
O'Connor D.,
Rhen M.
Publication year - 1990
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1990.tb02014.x
Subject(s) - biology , virulence , amino acid , bacterial outer membrane , mutant , mutagenesis , salmonella , plasmid , gene , arginine , peptide sequence , lipid a , biochemistry , escherichia coli , genetics , microbiology and biotechnology , bacteria
Summary The nucieotide sequence of the traT gene present in the virulence‐associated pfasmid of Salmonella typhimurium was determined. The predicted TraT protein encoded by this gene was found to consist of 243 amino acids and to resemble the known TraT proteins of the plasmids of the F incompatibility group. Thus it contains a signal sequence of 20 amino acids, an amino‐terminal lipid attachment site, and two strongly hydrophobic regions close to each other in the mature protein. A mutation leading to increased permeability of the outer membrane to hydrophobic agents, previousfy focalrzed to the traT gene, was shown to change a glycine residue to arginine within one of these hydrophobic regions. The same principle was found to apply to TraT of R6‐5: the introduction, by site‐directed mutagenesis, of either positively or negatively charged amino acids or the helix‐disrupting proline in the corresponding hydrophobic region led to increased hydrophobic permeability of the outer membrane.