Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1985 Nov;164(2):544–549. doi: 10.1128/jb.164.2.544-549.1985

Regulation of Pseudomonas aeruginosa chemotaxis by the nitrogen source.

R Craven, T C Montie
PMCID: PMC214286  PMID: 3932326

Abstract

The regulation of amino acid chemotaxis by nitrogen was investigated in the gram-negative bacterium Pseudomonas aeruginosa. The quantitative capillary tube technique was used to measure chemotactic responses of bacteria to spatial gradients of amino acids and other attractants. Chemotaxis toward serine, arginine, and alpha-aminoisobutyrate was sharply dependent on the form in which nitrogen was presented to the bacteria. Bacteria grown on mineral salts-succinate with potassium nitrate gave responses to amino acids that were 2 to 3 times those of cells grown on ammonium sulfate and 10 to 20 times those of cells grown in mineral salts-succinate with Casamino Acids as the nitrogen source. A combination of ammonium sulfate and glutamate was as effective as Casamino Acids in depressing serine taxis. The threshold concentration for alpha-aminoisobutyrate taxis was consistently lower in nitrate-grown bacteria than in ammonia-grown bacteria. Responsiveness to sodium succinate, however, was not subject to regulation by nitrogen, and glucose chemotaxis was inhibited, rather than enhanced, in nitrate-grown bacteria. These results indicate that chemotaxis of P. aeruginosa toward amino acids is subject to regulation by nitrogen and that this regulation probably is expressed at the level of the chemoreceptors or transducers.

Full text

PDF
544

Selected References

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

  1. Aksamit R. R., Koshland D. E., Jr Identification of the ribose binding protein as the receptor for ribose chemotaxis in Salmonella typhimurium. Biochemistry. 1974 Oct 22;13(22):4473–4478. doi: 10.1021/bi00719a001. [DOI] [PubMed] [Google Scholar]
  2. Clarke S., Koshland D. E., Jr Membrane receptors for aspartate and serine in bacterial chemotaxis. J Biol Chem. 1979 Oct 10;254(19):9695–9702. [PubMed] [Google Scholar]
  3. Craven R. C., Montie T. C. Chemotaxis of Pseudomonas aeruginosa: involvement of methylation. J Bacteriol. 1983 May;154(2):780–786. doi: 10.1128/jb.154.2.780-786.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Harwood C. S., Rivelli M., Ornston L. N. Aromatic acids are chemoattractants for Pseudomonas putida. J Bacteriol. 1984 Nov;160(2):622–628. doi: 10.1128/jb.160.2.622-628.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hazelbauer G. L., Adler J. Role of the galactose binding protein in chemotaxis of Escherichia coli toward galactose. Nat New Biol. 1971 Mar 24;230(12):101–104. doi: 10.1038/newbio230101a0. [DOI] [PubMed] [Google Scholar]
  6. Hazelbauer G. L. Maltose chemoreceptor of Escherichia coli. J Bacteriol. 1975 Apr;122(1):206–214. doi: 10.1128/jb.122.1.206-214.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hedblom M. L., Adler J. Chemotactic response of Escherichia coli to chemically synthesized amino acids. J Bacteriol. 1983 Sep;155(3):1463–1466. doi: 10.1128/jb.155.3.1463-1466.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hedblom M. L., Adler J. Genetic and biochemical properties of Escherichia coli mutants with defects in serine chemotaxis. J Bacteriol. 1980 Dec;144(3):1048–1060. doi: 10.1128/jb.144.3.1048-1060.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Higgins C. F., Ames G. F. Regulatory regions of two transport operons under nitrogen control: nucleotide sequences. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1083–1087. doi: 10.1073/pnas.79.4.1083. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Janssen D. B., Habets W. J., Marugg J. T., Van Der Drift C. Nitrogen control in Pseudomonas aeruginosa: mutants affected in the synthesis of glutamine synthetase, urease, and NADP-dependent glutamate dehydrogenase. J Bacteriol. 1982 Jul;151(1):22–28. doi: 10.1128/jb.151.1.22-28.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Janssen D. B., Herst P. M., Joosten H. M., van der Drift C. Nitrogen control in Pseudomonas aeruginosa: a role for glutamine in the regulations of the synthesis of nadp-dependent glutamate dehydrogenase, urease and histidase. Arch Microbiol. 1981 Feb;128(4):398–402. doi: 10.1007/BF00405920. [DOI] [PubMed] [Google Scholar]
  12. Kay W. W., Gronlund A. F. Influence of carbon or nitrogen starvation on amino acid transport in Pseudomonas aeruginosa. J Bacteriol. 1969 Oct;100(1):276–282. doi: 10.1128/jb.100.1.276-282.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Koshland D. E., Jr, Anderson M. J. Effect of catabolite repression on chemotaxis in Salmonella typhimurium. Mol Biol Biochem Biophys. 1980;32:136–143. doi: 10.1007/978-3-642-81503-4_10. [DOI] [PubMed] [Google Scholar]
  14. Koshland D. E., Jr Biochemistry of sensing and adaptation in a simple bacterial system. Annu Rev Biochem. 1981;50:765–782. doi: 10.1146/annurev.bi.50.070181.004001. [DOI] [PubMed] [Google Scholar]
  15. Kustu S. G., McFarland N. C., Hui S. P., Esmon B., Ames G. F. Nitrogen control of Salmonella typhimurium: co-regulation of synthesis of glutamine synthetase and amino acid transport systems. J Bacteriol. 1979 Apr;138(1):218–234. doi: 10.1128/jb.138.1.218-234.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Lamartiniere C. A., Itoh H., Dempsey W. B. -dialkylamino acid transaminase from Pseudomonas cepacia. Purification, crystallization, physical, and kinetic properties. Biochemistry. 1971 Dec 7;10(25):4783–4788. doi: 10.1021/bi00801a028. [DOI] [PubMed] [Google Scholar]
  17. Mercenier A., Simon J. P., Haas D., Stalon V. Catabolism of L-arginine by Pseudomonas aeruginosa. J Gen Microbiol. 1980 Feb;116(2):381–389. doi: 10.1099/00221287-116-2-381. [DOI] [PubMed] [Google Scholar]
  18. Mesibov R., Ordal G. W., Adler J. The range of attractant concentrations for bacterial chemotaxis and the threshold and size of response over this range. Weber law and related phenomena. J Gen Physiol. 1973 Aug;62(2):203–223. doi: 10.1085/jgp.62.2.203. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Moulton R. C., Montie T. C. Chemotaxis by Pseudomonas aeruginosa. J Bacteriol. 1979 Jan;137(1):274–280. doi: 10.1128/jb.137.1.274-280.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Potts J. R., Clarke P. H. The effect of nitrogen limitation on catabolite repression of amidase, histidase and urocanase in Pseudomonas aeruginosa. J Gen Microbiol. 1976 Apr;93(2):377–387. doi: 10.1099/00221287-93-2-377. [DOI] [PubMed] [Google Scholar]
  21. Sias S. R., Ingraham J. L. Isolation and analysis of mutants of Pseudomonas aeruginosa unable to assimilate nitrate. Arch Microbiol. 1979 Sep;122(3):263–270. doi: 10.1007/BF00411289. [DOI] [PubMed] [Google Scholar]
  22. Stinson M. W., Cohen M. A., Merrick J. M. Isolation of dicarboxylic acid- and glucose-binding proteins from Pseudomonas aeruginosa. J Bacteriol. 1976 Nov;128(2):573–579. doi: 10.1128/jb.128.2.573-579.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Stinson M. W., Cohen M. A., Merrick J. M. Purification and properties of the periplasmic glucose-binding protein of Pseudomonas aeruginosa. J Bacteriol. 1977 Aug;131(2):672–681. doi: 10.1128/jb.131.2.672-681.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Taylor B. L. Role of proton motive force in sensory transduction in bacteria. Annu Rev Microbiol. 1983;37:551–573. doi: 10.1146/annurev.mi.37.100183.003003. [DOI] [PubMed] [Google Scholar]
  25. Terracciano J. S., Canale-Parola E. Enhancement of chemotaxis in Spirochaeta aurantia grown under conditions of nutrient limitation. J Bacteriol. 1984 Jul;159(1):173–178. doi: 10.1128/jb.159.1.173-178.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Wang E. A., Koshland D. E., Jr Receptor structure in the bacterial sensing system. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7157–7161. doi: 10.1073/pnas.77.12.7157. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES