Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1989 Nov;171(11):5860–5865. doi: 10.1128/jb.171.11.5860-5865.1989

Fine-structure genetic map of the maltose transport operon of Salmonella typhimurium.

E Schneider 1, L Bishop 1, E Schneider 1, V Alfandary 1, G F Ames 1
PMCID: PMC210446  PMID: 2553663

Abstract

We have constructed a fine-structure genetic map of the maltose transport operon in Salmonella typhimurium. We have isolated mal mutants by using indicator plates, penicillin selection, or a proton suicide technique. Mutants were obtained as spontaneous events or were induced by chemical mutagenesis and transposon insertion. Tn10 and Mu d(lac Ap)1 insertion mutations were used to create deletions. Mutations were also obtained in a gene that is equivalent to lamB in Escherichia coli, which codes for the lambda bacteriophage receptor. The gene products in the mutants were characterized by sodium dodecyl sulfate-polyacrylamide-gel electrophoresis and immunoblotting. Our data indicate that the location of this operon on the Salmonella chromosome as well as the gene order and its orientation are the same as those in E. coli. This map will be useful in studying the mechanism of periplasmic transport in S. typhimurium.

Full text

PDF
5860

Images in this article

5864Image
on p.5864

Selected References

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

  1. Ames G. F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu Rev Biochem. 1986;55:397–425. doi: 10.1146/annurev.bi.55.070186.002145. [DOI] [PubMed] [Google Scholar]
  2. Ames G. F., Nikaido K., Groarke J., Petithory J. Reconstitution of periplasmic transport in inside-out membrane vesicles. Energization by ATP. J Biol Chem. 1989 Mar 5;264(7):3998–4002. [PubMed] [Google Scholar]
  3. 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]
  4. Bochner B. R., Huang H. C., Schieven G. L., Ames B. N. Positive selection for loss of tetracycline resistance. J Bacteriol. 1980 Aug;143(2):926–933. doi: 10.1128/jb.143.2.926-933.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gilson E., Rousset J. P., Charbit A., Perrin D., Hofnung M. malM, a new gene of the maltose regulon in Escherichia coli K12. I. malM is the last gene of the malK-lamB operon and encodes a periplasmic protein. J Mol Biol. 1986 Oct 5;191(3):303–311. doi: 10.1016/0022-2836(86)90127-0. [DOI] [PubMed] [Google Scholar]
  6. Gutnick D., Calvo J. M., Klopotowski T., Ames B. N. Compounds which serve as the sole source of carbon or nitrogen for Salmonella typhimurium LT-2. J Bacteriol. 1969 Oct;100(1):215–219. doi: 10.1128/jb.100.1.215-219.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Harkki A., Karkku H., Palva E. T. Use of lambda vehicles to isolate ompC-lacZ gene fusions in Salmonella typhimurium LT2. Mol Gen Genet. 1987 Oct;209(3):607–611. doi: 10.1007/BF00331170. [DOI] [PubMed] [Google Scholar]
  8. Higgins C. F., Haag P. D., Nikaido K., Ardeshir F., Garcia G., Ames G. F. Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium. Nature. 1982 Aug 19;298(5876):723–727. doi: 10.1038/298723a0. [DOI] [PubMed] [Google Scholar]
  9. Hobson A. C., Weatherwax R., Ames G. F. ATP-binding sites in the membrane components of histidine permease, a periplasmic transport system. Proc Natl Acad Sci U S A. 1984 Dec;81(23):7333–7337. doi: 10.1073/pnas.81.23.7333. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Joshi A. K., Ahmed S., Ferro-Luzzi Ames G. Energy coupling in bacterial periplasmic transport systems. Studies in intact Escherichia coli cells. J Biol Chem. 1989 Feb 5;264(4):2126–2133. [PubMed] [Google Scholar]
  11. Kleckner N., Chan R. K., Tye B. K., Botstein D. Mutagenesis by insertion of a drug-resistance element carrying an inverted repetition. J Mol Biol. 1975 Oct 5;97(4):561–575. doi: 10.1016/s0022-2836(75)80059-3. [DOI] [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. Madonna M. J., Fuchs R. L., Brenchley J. E. Fine structure analysis of Salmonella typhimurium glutamate synthase genes. J Bacteriol. 1985 Jan;161(1):353–360. doi: 10.1128/jb.161.1.353-360.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Palva E. T. Major outer membrane protein in Salmonella typhimurium induced by maltose. J Bacteriol. 1978 Oct;136(1):286–294. doi: 10.1128/jb.136.1.286-294.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Palva E. T., Westermann P. Arrangement of the maltose-inducible major outer membrane proteins, the bacteriophage lambda receptor in Escherichia coli and the 44 K protein in Salmonella typhimurium. FEBS Lett. 1979 Mar 1;99(1):77–80. doi: 10.1016/0014-5793(79)80253-7. [DOI] [PubMed] [Google Scholar]
  16. Plate C. A. Requirement for membrane potential in active transport of glutamine by Escherichia coli. J Bacteriol. 1979 Jan;137(1):221–225. doi: 10.1128/jb.137.1.221-225.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Prossnitz E., Nikaido K., Ulbrich S. J., Ames G. F. Formaldehyde and photoactivatable cross-linking of the periplasmic binding protein to a membrane component of the histidine transport system of Salmonella typhimurium. J Biol Chem. 1988 Dec 5;263(34):17917–17920. [PubMed] [Google Scholar]
  18. Raibaud O., Roa M., Braun-Breton C., Schwartz M. Structure of the malB region in Escherichia coli K12. I. Genetic map of the malK-lamB operon. Mol Gen Genet. 1979 Jul 24;174(3):241–248. doi: 10.1007/BF00267796. [DOI] [PubMed] [Google Scholar]
  19. Sanderson K. E., Roth J. R. Linkage map of Salmonella typhimurium, edition VII. Microbiol Rev. 1988 Dec;52(4):485–532. doi: 10.1128/mr.52.4.485-532.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Winkelman J. W., Clark D. P. Proton suicide: general method for direct selection of sugar transport- and fermentation-defective mutants. J Bacteriol. 1984 Nov;160(2):687–690. doi: 10.1128/jb.160.2.687-690.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES