Molecular and General Genetics MGG

, Volume 181, Issue 3, pp 338–345 | Cite as

Fluorocitrate resistant tricarboxylate transport mutants of Salmonella typhimurium

  • J. M. Somers
  • G. D. Sweet
  • W. W. Kay


Spontaneous and Tn10 induced fluorocitrate resistant mutants were isolated and characterized. These mutants were unable to grow on either cis-aconitate or DL-isocitrate but were still able to grow slowly on sodium citrate and normally on potassium or potassium-plus-sodium citrate. These mutants were defective in both citrate transport and citrate binding to periplasmic proteins. Tn10 insertion mutants were unable to produce immunologically detectable amounts of the citrate inducible periplasmic C protein previously shown to bind tricarboxylates.

Using a series of tct::Tn10 directed Hfrs the tct locus was accurately positioned at 59 units between srlA and pheA, but was not cotransducible with either gene. In the absence of P22 mediated cotransduction with 16 adjacent chromosomal markers the srlA and tct loci were bridged by using a series of tct flanking Tn10 insertions, and by newly isolated and characterized nalB mutants. In addition the hyd and recA loci were located establishing the gene order in this region of the chromosome as: pheA tct nalB recA srlA hyd cys. Nitrosoguanidine derived tricarboxylate mutations (Imai 1975) were also mapped within the tct locus.


Sodium Potassium Citrate Sodium Citrate Gene Order 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Abou-Jaoude A, Pascal MC, Casse F, Chippaux M (1978) Isolation and phenotypes of mutants from Escherichia coli K12 defective in nitrite reductase activity. FEMS Microbiol Lett 3:235–239Google Scholar
  2. Ames GF (1974) Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. Membrane, soluble, and periplasmic fractions. J Biol Chem 249:634–644Google Scholar
  3. Ashton DM, Sweet GD, Somers JM, Kay WW (1980) Citrate transport in Salmonella typhimurium: studies with 2-fluoro-L-erythro-citrate as a substrate. Can J Biochem 58:797–803Google Scholar
  4. Chan RK, Botstein D, Watanabe T, Ogata Y (1972) Specialized transduction of tetracycline resistance by phage P22 in Salmonella typhimurium. II. Properties of a high-frequency-transducing lysate. Virology 50:883–898Google Scholar
  5. Chumley FG, Menzel R, Roth JR (1979) Hfr formation directed by Tn10. Genetics 91, 639–655Google Scholar
  6. Frost GE, Rosenberg H (1973) The citrate-dependent iron transport system in Escherichia coli K-12. Biochim Biophys. Acta 330:90–101Google Scholar
  7. Hane MW, Wood TH (1969) Escherichia coli mutants resistant to nalidixic acid: genetic mapping and dominance studies. J Bacteriol 99:238–241Google Scholar
  8. Hancock REW, Hantke K, Braun V (1976) Iron transport in Escherichia coli K12: involvement of the colicin B receptor and of a citrate-inducible protein. J Bacteriol 127:1370–1375Google Scholar
  9. Imai K (1975) Isolation of tricarboxylate transport-negative mutants of Salmonella typhimurium. J Gen Appl Microbiol 21:127–134Google Scholar
  10. Imai K, Iijima T, Banno I (1977) Location of tct (tricarboxylic acid transport) genes on the chromosome of Salmonella typhimurium. Inst Ferment Res Commun (Osaka) 8:63–68Google Scholar
  11. Ingolia TJ, Koshland Jr, DE (1979) Response to a metal ion citrate complex in bacterial sensing. J Bacteriol 140:798–804Google Scholar
  12. Kay WW (1978) Carboxylic acid transport. In: Rosen BP (ed) Bacterial transport. Marcel Dekker, Inc, New York, p 385Google Scholar
  13. Kay WW, Cameron M (1978) Citrate transport in Salmonella typhimurium. Arch Biochem Biophys 190:270–278Google Scholar
  14. Kemper J (1974) Gene order and co-transduction in the leu-ara-fob-pyrA region of Salmonella typhimurium linkage map. J Bacteriol 117:94–99Google Scholar
  15. Kihara M, Macnab RM (1979) Chemotaxis of Salmonella typhimurium toward citrate. J Bacteriol 140:297–300Google Scholar
  16. Kleckner N, Chan RK, Tye B, Botstein D (1975) Mutagenesis by insertion of a drug-resistance element carrying an inverted repetition. J Mol Biol 97:561–575Google Scholar
  17. Kleckner N, Roth J, Botstein D (1977) Genetic engineering in vivo using translocatable drug-resistance elements. New methods in bacterial genetics. J Mol Biol 116:125–159Google Scholar
  18. Kleckner N, Reichardt K, Botstein D (1979) Inversions and deletions of the Salmonella chromosome generated by the translocatable tetracycline resistance element Tn10. J Mol Biol 127:89–115Google Scholar
  19. Sanderson KE, Hartman P (1978) Linkage map of Salmonella typhimurium. Microbiol Rev 42:471–519Google Scholar
  20. Sweet GD, Somers JM, Kay WW (1979) Purification and properties of a citrate-binding transport component, the C protein of Salmonella typhimurium. Can J Biochem 57:710–715Google Scholar
  21. Willis RE, Morris RG, Cirakoglu C, Schellenerg GD, Gerber NH, Furlong CE (1975) Preparation of the periplasmic binding proteins from Salmonella typhimurium and Escherichia coli. Arch Biochem Biophys 161:64–75Google Scholar

Copyright information

© Springer-Verlag 1981

Authors and Affiliations

  • J. M. Somers
    • 1
  • G. D. Sweet
    • 1
  • W. W. Kay
    • 1
  1. 1.Department of Biochemistry and MicrobiologyUniversity of VictoriaVictoriaCanada

Personalised recommendations