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. 1997 Feb;63(2):567–573. doi: 10.1128/aem.63.2.567-573.1997

L-Arogenate Is a Chemoattractant Which Can Be Utilized as the Sole Source of Carbon and Nitrogen by Pseudomonas aeruginosa

R S Fischer, J Song, W Gu, R A Jensen
PMCID: PMC1389519  PMID: 16535513

Abstract

L-Arogenate is a commonplace amino acid in nature in consideration of its role as a ubiquitous precursor of L-phenylalanine and/or L-tyrosine. However, the questions of whether it serves as a chemoattractant molecule and whether it can serve as a substrate for catabolism have never been studied. We found that Pseudomonas aeruginosa recognizes L-arogenate as a chemoattractant molecule which can be utilized as a source of both carbon and nitrogen. Mutants lacking expression of either cyclohexadienyl dehydratase or phenylalanine hydroxylase exhibited highly reduced growth rates when utilizing L-arogenate as a nitrogen source. Utilization of L-arogenate as a source of either carbon or nitrogen was dependent upon (sigma)(sup54), as revealed by the use of an rpoN null mutant. The evidence suggests that catabolism of L-arogenate proceeds via alternative pathways which converge at 4-hydroxyphenylpyruvate. In one pathway, prephenate formed in the periplasm by deamination of L-arogenate is converted to 4-hydroxyphenylpyruvate by cyclohexadienyl dehydrogenase. The second route depends upon the sequential action of periplasmic cyclohexadienyl dehydratase, phenylalanine hydroxylase, and aromatic aminotransferase.

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Selected References

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

  1. Adler J. A method for measuring chemotaxis and use of the method to determine optimum conditions for chemotaxis by Escherichia coli. J Gen Microbiol. 1973 Jan;74(1):77–91. doi: 10.1099/00221287-74-1-77. [DOI] [PubMed] [Google Scholar]
  2. Bonner C. A., Fischer R. S., Ahmad S., Jensen R. A. Remnants of an ancient pathway to L-phenylalanine and L-tyrosine in enteric bacteria: evolutionary implications and biotechnological impact. Appl Environ Microbiol. 1990 Dec;56(12):3741–3747. doi: 10.1128/aem.56.12.3741-3747.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bonner C., Jensen R. Prephenate aminotransferase. Methods Enzymol. 1987;142:479–487. doi: 10.1016/s0076-6879(87)42059-4. [DOI] [PubMed] [Google Scholar]
  4. Craven R., Montie T. C. Regulation of Pseudomonas aeruginosa chemotaxis by the nitrogen source. J Bacteriol. 1985 Nov;164(2):544–549. doi: 10.1128/jb.164.2.544-549.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fischer R. S., Berry A., Gaines C. G., Jensen R. A. Comparative action of glyphosate as a trigger of energy drain in eubacteria. J Bacteriol. 1986 Dec;168(3):1147–1154. doi: 10.1128/jb.168.3.1147-1154.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fiske M. J., Whitaker R. J., Jensen R. A. Hidden overflow pathway to L-phenylalanine in Pseudomonas aeruginosa. J Bacteriol. 1983 May;154(2):623–631. doi: 10.1128/jb.154.2.623-631.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. HOLLOWAY B. W. Genetic recombination in Pseudomonas aeruginosa. J Gen Microbiol. 1955 Dec;13(3):572–581. doi: 10.1099/00221287-13-3-572. [DOI] [PubMed] [Google Scholar]
  8. Hsing W., Canale-Parola E. Cellobiose chemotaxis by the cellulolytic bacterium Cellulomonas gelida. J Bacteriol. 1992 Dec;174(24):7996–8002. doi: 10.1128/jb.174.24.7996-8002.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Jensen R., Fischer R. The postprephenate biochemical pathways to phenylalanine and tyrosine: an overview. Methods Enzymol. 1987;142:472–478. doi: 10.1016/s0076-6879(87)42058-2. [DOI] [PubMed] [Google Scholar]
  10. Kamoun S., Kado C. I. Phenotypic Switching Affecting Chemotaxis, Xanthan Production, and Virulence in Xanthomonas campestris. Appl Environ Microbiol. 1990 Dec;56(12):3855–3860. doi: 10.1128/aem.56.12.3855-3860.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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]
  12. Mesibov R., Adler J. Chemotaxis toward amino acids in Escherichia coli. J Bacteriol. 1972 Oct;112(1):315–326. doi: 10.1128/jb.112.1.315-326.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Moench T. T., Konetzka W. A. Chemotaxis in Pseudomonas aeruginosa. J Bacteriol. 1978 Jan;133(1):427–429. doi: 10.1128/jb.133.1.427-429.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. 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]
  15. Ordal G. W., Villani D. P., Rosendahl M. S. Chemotaxis towards sugars by Bacillus subtilis. J Gen Microbiol. 1979 Nov;115(1):167–172. doi: 10.1099/00221287-115-1-167. [DOI] [PubMed] [Google Scholar]
  16. Patel N., Pierson D. L., Jensen R. A. Dual enzymatic routes to L-tyrosine and L-phenylalanine via pretyrosine in Pseudomonas aeruginosa. J Biol Chem. 1977 Aug 25;252(16):5839–5846. [PubMed] [Google Scholar]
  17. Song J., Jensen R. A. PhhR, a divergently transcribed activator of the phenylalanine hydroxylase gene cluster of Pseudomonas aeruginosa. Mol Microbiol. 1996 Nov;22(3):497–507. doi: 10.1046/j.1365-2958.1996.00131.x. [DOI] [PubMed] [Google Scholar]
  18. Totten P. A., Lara J. C., Lory S. The rpoN gene product of Pseudomonas aeruginosa is required for expression of diverse genes, including the flagellin gene. J Bacteriol. 1990 Jan;172(1):389–396. doi: 10.1128/jb.172.1.389-396.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Whitaker R. J., Gaines C. G., Jensen R. A. A multispecific quintet of aromatic aminotransferases that overlap different biochemical pathways in Pseudomonas aeruginosa. J Biol Chem. 1982 Nov 25;257(22):13550–13556. [PubMed] [Google Scholar]
  20. Xia T. H., Jensen R. A. A single cyclohexadienyl dehydrogenase specifies the prephenate dehydrogenase and arogenate dehydrogenase components of the dual pathways to L-tyrosine in Pseudomonas aeruginosa. J Biol Chem. 1990 Nov 15;265(32):20033–20036. [PubMed] [Google Scholar]
  21. Xia T., Song J., Zhao G., Aldrich H., Jensen R. A. The aroQ-encoded monofunctional chorismate mutase (CM-F) protein is a periplasmic enzyme in Erwinia herbicola. J Bacteriol. 1993 Aug;175(15):4729–4737. doi: 10.1128/jb.175.15.4729-4737.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Zamir L. O., Tiberio R., Fiske M., Berry A., Jensen R. A. Enzymatic and nonenzymatic dehydration reactions of L-arogenate. Biochemistry. 1985 Mar 26;24(7):1607–1612. doi: 10.1021/bi00328a006. [DOI] [PubMed] [Google Scholar]
  23. Zhao G. S., Xia T. H., Fischer R. S., Jensen R. A. Cyclohexadienyl dehydratase from Pseudomonas aeruginosa. Molecular cloning of the gene and characterization of the gene product. J Biol Chem. 1992 Feb 5;267(4):2487–2493. [PubMed] [Google Scholar]
  24. Zhao G., Xia T., Aldrich H., Jensen R. A. Cyclohexadienyl dehydratase from Pseudomonas aeruginosa is a periplasmic protein. J Gen Microbiol. 1993 Apr;139(4):807–813. doi: 10.1099/00221287-139-4-807. [DOI] [PubMed] [Google Scholar]
  25. Zhao G., Xia T., Song J., Jensen R. A. Pseudomonas aeruginosa possesses homologues of mammalian phenylalanine hydroxylase and 4 alpha-carbinolamine dehydratase/DCoH as part of a three-component gene cluster. Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1366–1370. doi: 10.1073/pnas.91.4.1366. [DOI] [PMC free article] [PubMed] [Google Scholar]

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