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Periplasmic protein associated with the oligopeptide permeases of Salmonella typhimurium and Escherichia coli.

Journal of Bacteriology, 01 Sep 1983, 155(3):1434-1438
https://doi.org/10.1128/jb.155.3.1434-1438.1983 PMID: 6350270 PMCID: PMC217845

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Abstract 

A periplasmic protein essential for the function of the oligopeptide transport system of Salmonella typhimurium was identified. This protein, encoded by the oppA gene, is one of the most abundant proteins in the periplasm and, with an apparent molecular weight of 52,000, is considerably larger than any other known periplasmic transport component. A similarly abundant periplasmic protein forms part of the oligopeptide transport system of Escherichia coli.

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J Bacteriol. 1983 Sep; 155(3): 1434–1438.
PMCID: PMC217845
PMID: 6350270

Periplasmic protein associated with the oligopeptide permeases of Salmonella typhimurium and Escherichia coli.

C F Higgins and M M Hardie
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Abstract

A periplasmic protein essential for the function of the oligopeptide transport system of Salmonella typhimurium was identified. This protein, encoded by the oppA gene, is one of the most abundant proteins in the periplasm and, with an apparent molecular weight of 52,000, is considerably larger than any other known periplasmic transport component. A similarly abundant periplasmic protein forms part of the oligopeptide transport system of Escherichia coli.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Ames GF. Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. Membrane, soluble, and periplasmic fractions. J Biol Chem. 1974 Jan 25;249(2):634–644. [Abstract] [Google Scholar]
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  • Higgins CF, Ames GF. Two periplasmic transport proteins which interact with a common membrane receptor show extensive homology: complete nucleotide sequences. Proc Natl Acad Sci U S A. 1981 Oct;78(10):6038–6042. [Europe PMC free article] [Abstract] [Google Scholar]
  • Higgins CF, Hardie MM, Jamieson D, Powell LM. Genetic map of the opp (Oligopeptide permease) locus of Salmonella typhimurium. J Bacteriol. 1983 Feb;153(2):830–836. [Europe PMC free article] [Abstract] [Google Scholar]
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  • Noel D, Nikaido K, Ames GF. A single amino acid substitution in a histidine-transport protein drastically alters its mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochemistry. 1979 Sep 18;18(19):4159–4165. [Abstract] [Google Scholar]
  • Nossal NG, Heppel LA. The release of enzymes by osmotic shock from Escherichia coli in exponential phase. J Biol Chem. 1966 Jul 10;241(13):3055–3062. [Abstract] [Google Scholar]
  • Payne JW, Bell G. Direct determination of the properties of peptide transport systems in Escherichia coli, using a fluorescent-labeling procedure. J Bacteriol. 1979 Jan;137(1):447–455. [Europe PMC free article] [Abstract] [Google Scholar]
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