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PMID: 3323837 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Amino acid alterations in a hydrophobic region of the TraT protein of R6-5 increase the outer membrane permeability of enteric bacteria.

Molecular & general genetics : MGG ·Vol. 210 ·No. 1 ·1987-11-00 ·Pages 178-80

Sukupolvi S, O'Connor D

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.

MeSH Terms
Amino Acid Sequence Bacterial Outer Membrane Proteins/genetics,metabolism Cell Membrane Permeability Escherichia coli/genetics,metabolism Escherichia coli Proteins Genes, Bacterial Molecular Sequence Data Mutation Plasmids Salmonella typhimurium/genetics,metabolism
Chemicals
Bacterial Outer Membrane Proteins Escherichia coli Proteins TraT protein, E coli
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sukupolvi S
National Public Health Institute, Helsinki, Finland.
O'Connor D
References (15)
15 references, click to expand
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Article Info
Journal
Molecular & general genetics : MGG
Abbr.
Mol Gen Genet
ISSN
0026-8925
DOI
10.1007/BF00337776
Published
1987-11-00
Pages
178-80
Language
English
Region
Germany
NLM ID
0125036
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00337776
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