Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1978 Nov;75(11):5447–5451. doi: 10.1073/pnas.75.11.5447

Identification of a membrane protein as a histidine transport component in Salmonella typhimurium.

G F Ames, K Nikaido
PMCID: PMC392981  PMID: 364482

Abstract

A component of high-affinity histidine transport in Salmonella typhimurium has been identified. It is a basic (pI about 9.0) membrane-bound protein, the P protein. It is shown to be coded for by the distal half of the previously described hisP gene by analysis of numerous hisP mutants, two of which exhibit P proteins with altered electrophoretic mobilities. Upon separation of the cytoplasmic (inner) from the outer membrane, it can be shown that the P protein is located in the cytoplasmic membrane. The P protein is under the same regulatory controls as histidine transport--i.e., transport operon promoter dhuA and nitrogen regulation. A wild-type cell contains about 200 molecules of P protein. As a result of this work we now divide the hisP gene into two genes: the hisP gene proper and the hisQ gene, which codes for another essential component of histidine transport, the Q protein. The P protein was shown previously by genetic analysis to interact with the periplasmic histidine-binding protein J, another essential component of histidine transport. Possible mechanism for the interaction of the J, P, and Q components in histidine transport, and of P and Q in lysine/arginine/ornithine transport, are discussed.

Full text

PDF
5447

Images in this article

5448Image
on p.5448
5449Image
on p.5449
5450Image
on p.5450

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AMES G. F. UPTAKE OF AMINO ACIDS BY SALMONELLA TYPHIMURIUM. Arch Biochem Biophys. 1964 Jan;104:1–18. doi: 10.1016/s0003-9861(64)80028-x. [DOI] [PubMed] [Google Scholar]
  2. Ames G. F., Lever J. Components of histidine transport: histidine-binding proteins and hisP protein. Proc Natl Acad Sci U S A. 1970 Aug;66(4):1096–1103. doi: 10.1073/pnas.66.4.1096. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ames G. F., Nikaido K. Two-dimensional gel electrophoresis of membrane proteins. Biochemistry. 1976 Feb 10;15(3):616–623. doi: 10.1021/bi00648a026. [DOI] [PubMed] [Google Scholar]
  4. Ames G. F., Noel K. D., Taber H., Spudich E. N., Nikaido K., Afong J. Fine-structure map of the histidine transport genes in Salmonella typhimurium. J Bacteriol. 1977 Mar;129(3):1289–1297. doi: 10.1128/jb.129.3.1289-1297.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ames G. F. 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. [PubMed] [Google Scholar]
  6. Ames G. F., Spudich E. N., Nikaido H. Protein composition of the outer membrane of Salmonella typhimurium: effect of lipopolysaccharide mutations. J Bacteriol. 1974 Feb;117(2):406–416. doi: 10.1128/jb.117.2.406-416.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ames G. F., Spurich E. N. Protein-protein interaction in transport: periplasmic histidine-binding protein J interacts with P protein. Proc Natl Acad Sci U S A. 1976 Jun;73(6):1877–1881. doi: 10.1073/pnas.73.6.1877. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  9. Boos W. Bacterial transport. Annu Rev Biochem. 1974;43(0):123–146. doi: 10.1146/annurev.bi.43.070174.001011. [DOI] [PubMed] [Google Scholar]
  10. Fox C. F., Carter J. R., Kennedy E. P. GENETIC CONTROL OF THE MEMBRANE PROTEIN COMPONENT OF THE LACTOSE TRANSPORT SYSTEM OF Escherichia coli. Proc Natl Acad Sci U S A. 1967 Mar;57(3):698–705. doi: 10.1073/pnas.57.3.698. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hirata H., Sone N., Yoshida M., Kagawa Y. Isolation of the alanine carrier from the membranes of a thermophilic bacterium and its reconstitution into vesicles capable of transport. J Supramol Struct. 1977;6(1):77–84. doi: 10.1002/jss.400060106. [DOI] [PubMed] [Google Scholar]
  12. Kennedy E. P., Rumley M. K., Armstrong J. B. Dierect measurement of the binding of labeled sugars to the lactose permease M protein. J Biol Chem. 1974 Jan 10;249(1):33–37. [PubMed] [Google Scholar]
  13. Kustu S. G., Ames G. F. The hisP protein, a known histidine transport component in Salmonella typhimurium, is also an arginine transport component. J Bacteriol. 1973 Oct;116(1):107–113. doi: 10.1128/jb.116.1.107-113.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kustu S. G., Ames G. F. The histidine-binding protein J, a histidine transport component, has two different functional sites. J Biol Chem. 1974 Nov 10;249(21):6976–6983. [PubMed] [Google Scholar]
  15. Lever J. E. Purification and properties of a component of histidine transport in Salmonella typhimurium. The histidine-binding protein J. J Biol Chem. 1972 Jul 10;247(13):4317–4326. [PubMed] [Google Scholar]
  16. Lo T. C. The molecular mechanism of dicarboxylic acid transport in Escherichia coli K 12. J Supramol Struct. 1977;7(3-4):463–480. doi: 10.1002/jss.400070316. [DOI] [PubMed] [Google Scholar]
  17. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  18. O'Farrell P. Z., Goodman H. M., O'Farrell P. H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell. 1977 Dec;12(4):1133–1141. doi: 10.1016/0092-8674(77)90176-3. [DOI] [PubMed] [Google Scholar]
  19. Sanderson K. E., Hartman P. E. Linkage map of Salmonella typhimurium, edition V. Microbiol Rev. 1978 Jun;42(2):471–519. doi: 10.1128/mr.42.2.471-519.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Singer S. J. The molecular organization of membranes. Annu Rev Biochem. 1974;43(0):805–833. doi: 10.1146/annurev.bi.43.070174.004105. [DOI] [PubMed] [Google Scholar]
  21. Smit J., Kamio Y., Nikaido H. Outer membrane of Salmonella typhimurium: chemical analysis and freeze-fracture studies with lipopolysaccharide mutants. J Bacteriol. 1975 Nov;124(2):942–958. doi: 10.1128/jb.124.2.942-958.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Strange P. G., Koshland D. E., Jr Receptor interactions in a signalling system: competition between ribose receptor and galactose receptor in the chemotaxis response. Proc Natl Acad Sci U S A. 1976 Mar;73(3):762–766. doi: 10.1073/pnas.73.3.762. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Teather R. M., Müller-Hill B., Abrutsch U., Aichele G., Overath P. Amplification of the lactose carrier protein in Escherichia coli using a plasmid vector. Mol Gen Genet. 1978 Feb 27;159(3):239–248. doi: 10.1007/BF00268260. [DOI] [PubMed] [Google Scholar]
  24. Willis R. C., Furlong C. E. Purification and properties of a periplasmic glutamate-aspartate binding protein from Escherichia coli K12 strain W3092. J Biol Chem. 1975 Apr 10;250(7):2574–2580. [PubMed] [Google Scholar]
  25. Wittenberg J. B. Myoglobin-facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle. Physiol Rev. 1970 Oct;50(4):559–636. doi: 10.1152/physrev.1970.50.4.559. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES