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. 1990 May;172(5):2280–2286. doi: 10.1128/jb.172.5.2280-2286.1990

Regulation of tfdCDEF by tfdR of the 2,4-dichlorophenoxyacetic acid degradation plasmid pJP4.

B Kaphammer 1, J J Kukor 1, R H Olsen 1
PMCID: PMC208860  PMID: 2158967

Abstract

The closely linked structural genes tfdCDEF borne on the 2,4-dichlorophenoxyacetic acid (TFD) catabolic plasmid, pRO101, were cloned into vector pRO2321 as a 12.6-kilobase-pair BamHI C fragment and designated pRO2334. The first gene in this cluster, tfdC, encodes chlorocatechol 1,2-dioxygenase and was expressed constitutively. Chlorocatechol 1,2-dioxygenase expression by pRO2334 was repressed in trans by the negative regulatory element, tfdR, on plasmid pRO1949. Derepression of tfdC was achieved when Pseudomonas aeruginosa PAO4032 containing both plasmids pRO2334 and pRO1949 was grown in minimal glucose medium containing TFD, 2,4-dichlorophenol, or 4-chlorocatechol, suggesting that TFD and other pathway intermediates can act as inducing compounds. Genetic organization of the tfdCDEF cluster was established by deletion of the tfdC gene, which resulted in the loss of tfdD and tfdE activity, suggesting that genes tfdCDEF are organized in an operon transcribed from the negatively regulated promoter of tfdC. Deletion subcloning of pRO1949 was used to localize tfdR to a 1.2-kilobase-pair BamHI-XhoI region of the BamHI E fragment of plasmid pRO101. The tfdR gene product was shown not to regulate the expression of tfdB, which encodes 2,4-dichlorophenol hydroxylase.

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Selected References

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  1. Bird J. A., Cain R. B. cis-cis-Muconate, the product inducer of catechol 1,2-oxygenase in Pseudomonas aeruginosa. Biochem J. 1968 Sep;109(3):479–481. doi: 10.1042/bj1090479. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  3. Cuskey S. M., Peccoraro V., Olsen R. H. Initial catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO: pathway description, mapping of mutations, and cloning of essential genes. J Bacteriol. 1987 Jun;169(6):2398–2404. doi: 10.1128/jb.169.6.2398-2404.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cuskey S. M., Wolff J. A., Phibbs P. V., Jr, Olsen R. H. Cloning of genes specifying carbohydrate catabolism in Pseudomonas aeruginosa and Pseudomonas putida. J Bacteriol. 1985 Jun;162(3):865–871. doi: 10.1128/jb.162.3.865-871.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Don R. H., Pemberton J. M. Genetic and physical map of the 2,4-dichlorophenoxyacetic acid-degradative plasmid pJP4. J Bacteriol. 1985 Jan;161(1):466–468. doi: 10.1128/jb.161.1.466-468.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Don R. H., Pemberton J. M. Properties of six pesticide degradation plasmids isolated from Alcaligenes paradoxus and Alcaligenes eutrophus. J Bacteriol. 1981 Feb;145(2):681–686. doi: 10.1128/jb.145.2.681-686.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Don R. H., Weightman A. J., Knackmuss H. J., Timmis K. N. Transposon mutagenesis and cloning analysis of the pathways for degradation of 2,4-dichlorophenoxyacetic acid and 3-chlorobenzoate in Alcaligenes eutrophus JMP134(pJP4). J Bacteriol. 1985 Jan;161(1):85–90. doi: 10.1128/jb.161.1.85-90.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dorn E., Knackmuss H. J. Chemical structure and biodegradability of halogenated aromatic compounds. Two catechol 1,2-dioxygenases from a 3-chlorobenzoate-grown pseudomonad. Biochem J. 1978 Jul 15;174(1):73–84. doi: 10.1042/bj1740073. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Evans W. C., Smith B. S., Fernley H. N., Davies J. I. Bacterial metabolism of 2,4-dichlorophenoxyacetate. Biochem J. 1971 May;122(4):543–551. doi: 10.1042/bj1220543. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Fisher P. R., Appleton J., Pemberton J. M. Isolation and characterization of the pesticide-degrading plasmid pJP1 from Alcaligenes paradoxus. J Bacteriol. 1978 Sep;135(3):798–804. doi: 10.1128/jb.135.3.798-804.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ghosal D., You I. S., Chatterjee D. K., Chakrabarty A. M. Genes specifying degradation of 3-chlorobenzoic acid in plasmids pAC27 and pJP4. Proc Natl Acad Sci U S A. 1985 Mar;82(6):1638–1642. doi: 10.1073/pnas.82.6.1638. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Ghosal D., You I. S. Nucleotide homology and organization of chlorocatechol oxidation genes of plasmids pJP4 and pAC27. Mol Gen Genet. 1988 Jan;211(1):113–120. doi: 10.1007/BF00338401. [DOI] [PubMed] [Google Scholar]
  13. Henikoff S., Haughn G. W., Calvo J. M., Wallace J. C. A large family of bacterial activator proteins. Proc Natl Acad Sci U S A. 1988 Sep;85(18):6602–6606. doi: 10.1073/pnas.85.18.6602. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Holloway B. W., Krishnapillai V., Morgan A. F. Chromosomal genetics of Pseudomonas. Microbiol Rev. 1979 Mar;43(1):73–102. doi: 10.1128/mr.43.1.73-102.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kemp M. B., Hegeman G. D. Genetic control of the beta-ketoadipate pathway in Pseudomonas aeruginosa. J Bacteriol. 1968 Nov;96(5):1488–1499. doi: 10.1128/jb.96.5.1488-1499.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kojima Y., Fujisawa H., Nakazawa A., Nakazawa T., Kanetsuna F., Taniuchi H., Nozaki M., Hayaishi O. Studies on pyrocatechase. I. Purification and spectral properties. J Biol Chem. 1967 Jul 25;242(14):3270–3278. [PubMed] [Google Scholar]
  17. Kukor J. J., Olsen R. H., Ballou D. P. Cloning and expression of the catA and catBC gene clusters from Pseudomonas aeruginosa PAO. J Bacteriol. 1988 Oct;170(10):4458–4465. doi: 10.1128/jb.170.10.4458-4465.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Kukor J. J., Olsen R. H., Siak J. S. Recruitment of a chromosomally encoded maleylacetate reductase for degradation of 2,4-dichlorophenoxyacetic acid by plasmid pJP4. J Bacteriol. 1989 Jun;171(6):3385–3390. doi: 10.1128/jb.171.6.3385-3390.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Liu T., Chapman P. J. Purification and properties of a plasmid-encoded 2,4-dichlorophenol hydroxylase. FEBS Lett. 1984 Aug 6;173(2):314–318. doi: 10.1016/0014-5793(84)80797-8. [DOI] [PubMed] [Google Scholar]
  20. Meagher R. B., McCorkle G. M., Ornston M. K., Ornston L. N. Inducible uptake system for -carboxy-cis, cis-muconate in a permeability mutant of Pseudomonas putida. J Bacteriol. 1972 Aug;111(2):465–473. doi: 10.1128/jb.111.2.465-473.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Mercer A. A., Loutit J. S. Transformation and transfection of Pseudomonas aeruginosa: effects of metal ions. J Bacteriol. 1979 Oct;140(1):37–42. doi: 10.1128/jb.140.1.37-42.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Olsen R. H., DeBusscher G., McCombie W. R. Development of broad-host-range vectors and gene banks: self-cloning of the Pseudomonas aeruginosa PAO chromosome. J Bacteriol. 1982 Apr;150(1):60–69. doi: 10.1128/jb.150.1.60-69.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Olsen R. H., Hansen J. Evolution and utility of a Pseudomonas aeruginosa drug resistance factor. J Bacteriol. 1976 Mar;125(3):837–844. doi: 10.1128/jb.125.3.837-844.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Ornston L. N. The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. IV. Regulation. J Biol Chem. 1966 Aug 25;241(16):3800–3810. [PubMed] [Google Scholar]
  25. Perkins E. J., Bolton G. W., Gordon M. P., Lurquin P. F. Partial nucleotide sequence of the chlorocatechol degradative operon tfdCDEF of pJP4 and similarity to promoters of the chlorinated aromatic degradative operons tfdA and clcABD. Nucleic Acids Res. 1988 Jul 25;16(14B):7200–7200. doi: 10.1093/nar/16.14.7200. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Perkins E. J., Lurquin P. F. Duplication of a 2,4-dichlorophenoxyacetic acid monooxygenase gene in Alcaligenes eutrophus JMP134(pJP4). J Bacteriol. 1988 Dec;170(12):5669–5672. doi: 10.1128/jb.170.12.5669-5672.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Schell M. A., Sukordhaman M. Evidence that the transcription activator encoded by the Pseudomonas putida nahR gene is evolutionarily related to the transcription activators encoded by the Rhizobium nodD genes. J Bacteriol. 1989 Apr;171(4):1952–1959. doi: 10.1128/jb.171.4.1952-1959.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Schmidt E., Knackmuss H. J. Chemical structure and biodegradability of halogenated aromatic compounds. Conversion of chlorinated muconic acids into maleoylacetic acid. Biochem J. 1980 Oct 15;192(1):339–347. doi: 10.1042/bj1920339. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Stanier R. Y., Palleroni N. J., Doudoroff M. The aerobic pseudomonads: a taxonomic study. J Gen Microbiol. 1966 May;43(2):159–271. doi: 10.1099/00221287-43-2-159. [DOI] [PubMed] [Google Scholar]
  30. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  31. Wheelis M. L., Ornston L. N. Genetic control of enzyme induction in the -ketoadipate pathway of Pseudomonas putida: deletion mapping of cat mutations. J Bacteriol. 1972 Feb;109(2):790–795. doi: 10.1128/jb.109.2.790-795.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Zylstra G. J., Olsen R. H., Ballou D. P. Cloning, expression, and regulation of the Pseudomonas cepacia protocatechuate 3,4-dioxygenase genes. J Bacteriol. 1989 Nov;171(11):5907–5914. doi: 10.1128/jb.171.11.5907-5914.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]

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