1887

Abstract

Transposon Tn genomic mutants of plant-growth-promoting strain WCS358 have been isolated which no longer utilize ferulic and coumaric acids as sole sources of carbon and energy. Genetic studies confirmed previous biochemical data showing that ferulic acid is degraded via vanillic acid, and coumaric acid via hydroxybenzoic acid. The genes involved in these enzymic steps were cloned and characterized. Two proteins designated Fca (26.5 kDa) and Vdh (50.3 kDa) were identified as responsible for the conversion of ferulic acid to vanillic acid; the proteins are encoded by the and genes which are organized in an operon structure in the chromosome. The Vdh protein is 69% identical at the amino acid level to the Vdh protein recently identified in sp. strain HR199 and converts vanillin to vanillic acid. Homology studies revealed that the Vdh proteins exhibited significant identity to aldehyde dehydrogenases from different organisms whereas Fca belonged to the enoyl-CoA hydratase family of proteins. Two proteins, designated VanA (39.9 kDa) and VanB (34.3 kDa), encoded by two genes, and , are organized in an operon in the chromosome. They were found to be responsible for the demethylation of vanillic acid to protocatechuic acid. The VanA proteins showed no homology to any other known protein, while VanB belonged to the ferredoxin family of proteins. This two-component enzyme system demethylated another phenolic monomer, veratric acid, thus indicating broad specificity. Studies of the regulation of the operon demonstrated that the genes were induced by the substrate, vanillic acid; however, the strongest induction was observed when cells were grown in the presence of the product of the reaction, protocatechuic acid.

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1998-04-01
2021-05-09
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References

  1. Beringer J. E., Beynon J. L., Buchanan-Wollaston A. V., Johnston A. W. B. (1978); Transfer of the drug-resistance transposes Tn5 to Rhizobium.. Nature, 276:(5688),633–634 [CrossRef]
    [Google Scholar]
  2. Bernhardt F.-H., Pachowsky H., Staudinger H. (1975); A 4–methoxybenzoate O-demethylase from Pseudomonas putida. Eur J Biocbem, 57241–256
    [Google Scholar]
  3. Better M., Lewis B., Corbin D., Ditta G., Helinski D. R. (1983); Structural relationships among Rhizobium meliloti promoters. Cell, 35479–A85
    [Google Scholar]
  4. Birnboim H. C. (1983); A rapid alkaline extraction method for the isolation of plasmid DNA.. Methods in Enzymology, Vol 46: Research on Nitrification and Related Processes, Pt B, 100:243–255
    [Google Scholar]
  5. Bolton G. W., Nester E. W., Gordon M. P. (1986); Plant phenolic compounds induce expression of the Agrobacterium tumefaciens loci needed for virulence.. Science, 232:(4753),983–985 [CrossRef]
    [Google Scholar]
  6. Brunei F., Davison J. (1988); Cloning and sequencing of Pseudomonas genes encoding vanillate demethylase.. Journal of Bacteriology, 170:(10),4924–4930 [CrossRef]
    [Google Scholar]
  7. Bullock W. O., Fernandez J. M., Short J. M. (1987); XLl-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with betagalactosidase selection. Biotechniques 5,376—382.
  8. Buswell J., Ribbons D. W. (1988); Vanillate O-demethylase from Pseudomonas species.. Methods in Enzymology, Vol 46: Research on Nitrification and Related Processes, Pt B, 161:294–301
    [Google Scholar]
  9. Corbin D., Ditta G., Helinski D. R. (1982); Clustering of nitrogen fixation (nif) genes in Rhizobium meliloti.. Journal of Bacteriology, 149:(1),4759–4764 [CrossRef]
    [Google Scholar]
  10. Correl C. C., Batie C. J., Ballou D. P., Ludwig M. (1992); Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. Science, 2581604–1610
    [Google Scholar]
  11. Delneri D., Degrassi G., Rizzo R., Bruschi C. V. (1995); Degradation of trans-ferulic acid and p-coumaric acid by Acinetobacter calcoaceticus DSM 586. Biochimica Et Biophysica Acta, 1244363–367
    [Google Scholar]
  12. Deretic V., Chandrasekharappa S., Gill J. F., Chatterjee D. K., Chakrabarty A. M. (1987); A set of cassettes and improved vectors for genetic and biochemical characterization of Pseudomonas genes.. Gene, 57:(1),61–72 [CrossRef]
    [Google Scholar]
  13. Figurski D. H., Helinski D. R. (1979); Replication of an origin containing derivative of plasmid RK2 dependent on a plasmid function provided in trans.. Proc Natl Acad Sci USA, 76:(4),1648–1652 [CrossRef]
    [Google Scholar]
  14. Geels F. P., Schippers B. (1983); Reduction in yield depressions in high frequency potato cropping soil after seed tuber treatments with antagonistic fluorescent Pseudomonas spp.. Pbytopathol Z, 108:(3–4),207–221 [CrossRef]
    [Google Scholar]
  15. Hanahan D. (1983); Studies on transformation of Escherichia coli with plasmids.. } Mol Biol, 166:(4),557–580 [CrossRef]
    [Google Scholar]
  16. Kirk T. K., Farrell R. L. (1987); Enzymatic combustion’: the microbial degradation of lignin.. Annual Review of Microbiology, 41:(1),465–505 [CrossRef]
    [Google Scholar]
  17. Lawrence-Marsh J., Erfle M., Wykes E. J. (1984; The pIC plasmid and phage vectors with versatile cloning sites for recombinant selection by insertional inactivation. Gene, 32481–485
    [Google Scholar]
  18. Maniatis T., Fritsch E. F., Sambrook J. (1982) Molecular Cloning: a Laboratory Manual Cold Spring Harbor, NY:: Cold Spring Harbor Laboratory;
    [Google Scholar]
  19. Marugg J. D., van Spanje M., Hoekstra W. P. M., Schippers B., Weisbeek P. J. (1985); Isolation and analysis of genes involved in siderophore biosynthesis in plant-growth-stimulating Pseudomonas putida WCS358.. Journal of Bacteriology, 164:(2),563–570 [CrossRef]
    [Google Scholar]
  20. Mason J. R., Cammack R. (1992); The electron-transport proteins of hydroxylating bacterial dioxygenases.. Annual Review of Microbiology, 46:(1),277–305 [CrossRef]
    [Google Scholar]
  21. van der Meer J. F., de Vos W. M., Harayama S., Zehnder A. J. B. (1992); Molecular mechanisms of genetic adaptation to xenobiotic compounds.. Microbiological Reviews, 56:(4),677–694 [CrossRef]
    [Google Scholar]
  22. Melchers L. A., Regensburg-Tuink A. J. G., Schilperoort R. A., Hooykaas P. J. J. (1989); Specificity of signal molecules in the activation of Agrobacterium virulence gene expression.. Molecular Microbiology, 3:(7),969–977 [CrossRef]
    [Google Scholar]
  23. Messing J. (1983); New vectors for cloning.. Methods in Enzymology, Vol 46: Research on Nitrification and Related Processes, Pt B, 101:20–78
    [Google Scholar]
  24. Miller J. H. (1972) Experiments in Molecular Genetics Cold Spring Harbor, NY:: Cold Spring Harbor Laboratory;
    [Google Scholar]
  25. Minami-lshii N., Taketani S., Osumi T., Hashimoto T. (1989); Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. European Journal of Biochemistry, 18573–78
    [Google Scholar]
  26. Niedle E. L., Hartnett C., Ornston L. N., Bairoch A., Rekik M. et al. (1991); Nucleotide sequences of the Acinetobacter calcoaceticus ben ABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases.. Journal of Bacteriology, 173:(17),5385–5395 [CrossRef]
    [Google Scholar]
  27. Parke D. (1995); Supraoperonic clustering of pea genes for catabolism of the phenolic compound protocatechuate in Agrobacterium tumefaciens.. Journal of Bacteriology, 177:(13),3808–3817 [CrossRef]
    [Google Scholar]
  28. Priefert H., Rabnehorst J., Steinbuchel A. (1997); Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate.. ] Bacteriol, 179:(8),2595–2607 [CrossRef]
    [Google Scholar]
  29. Sanger F., Nicklen S., Coulson A. R. (1977); DNA sequencing with chain terminating inhibitors.. Proc Natl Acad Sci USA, 74:(12),5463–5467 [CrossRef]
    [Google Scholar]
  30. Sokatch J. R. (1986) The biology of Pseudomonas.. Edited by Sokatch J. R., Ornston L. In The Bacteria vol. X London:: Academic Press;27–133
    [Google Scholar]
  31. Spaink H. P., Okker R. J. H., Wijffelmann C. A., Pees E., Lugtenberg B. J. J. (1987); Promoter in the nodulation region of the Rhizobium leguminosarum Sym plasmid pRLlJI.. Plant Molecular Biology, 9:(1),27–39 [CrossRef]
    [Google Scholar]
  32. Stachel S. E., An G., Flores C., Nester E. W. (1985); A Tn3 lacZ transposon for the random generation of β-galactosidase gene fusions: application to the analysis of gene expression of Agrobacterium tumefaciens.. EMBO ], 4:(4),891–898 [CrossRef]
    [Google Scholar]
  33. Staskawicz B., Dahlbeck D., Keen N., Napoli C. (1987); Molecular characterization of cloned avirulence genes from race 0 and race 1 of Pseudomonas syringae pv. glycinea. Journal of Bacteriology, 1695789–5794
    [Google Scholar]
  34. Toms A., Wood J. M. (1970); The degradation of trans-ferulic acid by Pseudomonas acidovorans.. Biochemistry, 9:(2),337–343 [CrossRef]
    [Google Scholar]
  35. Venturi V., Ottevanger C., Bracke M., Weisbeek P. (1995); Iron regulation of siderophore biosynthesis and transport in Pseudomonas putida WCS358: involvement of a transcriptional activator and of the Fur protein. Molecular Microbiology, 151081–1094
    [Google Scholar]
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