1887

Abstract

The nucleotide sequence of the aromatic amine utilization () gene region from contained nine genes (, , , , and ) transcribed in the same direction. The and genes encode the periplasmic aromatic amine dehydrogenase (AADH) large and small subunit polypeptides, respectively, and were homologous to and , the genes for the large and small subunits of methylamine dehydrogenase (MADH). and are homologous to and and apparently carry out the same function of transport and folding of the small subunit polypeptide in the periplasm. No analogues of the , , , and genes responsible for biosynthesis of tryptophan tryptophylquinone (the prosthetic group of amine dehydrogenases) were found in the cluster. was predicted to encode a small periplasmic monohaem -type cytochrome. No biological function can be assigned to polypeptides encoded by , and and mutations in these genes appeared to be lethal. Mutants generated by insertions into were not able to use phenylethylamine, tyramine and tryptamine as a source of carbon and phenylethylamine, 3’-hydroxytyramine (dopamine) and tyramine as a source of nitrogen, indicating that AADH is the only enzyme involved in utilization of primary amines in . AADH genes are present in subsp. , but not in other β- and γ-proteobacteria. Phylogenetic analysis of amine dehydrogenases (MADH and AADH) indicated that AADH and MADH evolutionarily diverged before separation of proteobacteria into existing subclasses.

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2001-08-01
2024-12-07
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References

  1. Berks B. C. 1996; A common export pathway for proteins binding complex redox cofactor?. Mol Microbiol 22:393–404 [CrossRef]
    [Google Scholar]
  2. Busse H.-J., Auling G. 1992; The genera Alcaligenes and ‘ Achromobacter ’. In The Prokaryotes pp 2544–2555 Edited by Balows A., Harder W., Schleifer K.-H., Trüper H. G., Dworkin M. New York: Springer;
    [Google Scholar]
  3. Chen L., Mathews F. S., Davidson V. L., Huizinga E. G., Vellieux F. M. D., Duine J. A., Hol W. G. J. 1991; Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase. FEBS Lett 287:163–166 [CrossRef]
    [Google Scholar]
  4. Chistoserdov A. Y., Tsygankov Y. D., Lidstrom M. E. 1990; Cloning and sequencing of the structural gene for the small subunit of methylamine dehydrogenase from Methylobacterium extorquens AM1: evidence for two tryptophan residues involved in the active center. Biochem Biophys Res Commun 172:211–216 [CrossRef]
    [Google Scholar]
  5. Chistoserdov A. Y., Boyd J., Mathews F. S., Lidstrom M. E. 1992; The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans . Biochem Biophys Res Commun 184:1226–1234 [CrossRef]
    [Google Scholar]
  6. Chistoserdov A. Y., Chistoserdova L. V., McIntire W., Lidstrom M. E. 1994a; The organization of the mau gene cluster from Methylobacterium extorquens : complete nucleotide sequence and mutant characterization. J Bacteriol 176:4052–4065
    [Google Scholar]
  7. Chistoserdov A. Y., McIntire W., Mathews F. S., Lidstrom M. E. 1994b; The organization of the mau gene cluster from Methylophilus methylotrophus W3A1. J Bacteriol 176:4073–4080
    [Google Scholar]
  8. Ditta G., Schmidhauser T., Yakobson E., Lu P., Liang X. W., Finlay D. R., Guiney D., Helinski D. R. 1985; Plasmids related to the broad host range vector, pRK290, useful for gene cloning and for monitoring gene expression. Plasmid 13:149–153 [CrossRef]
    [Google Scholar]
  9. Eady R. R., Large P. J. 1968; Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine. Biochem J 106:245–255
    [Google Scholar]
  10. Edwards S. L., Davidson V. L., Hyun Y.-L., Wingfield P. T. 1995; Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes. J Biol Chem 270:4293–4298 [CrossRef]
    [Google Scholar]
  11. Gak E. R., Chistoserdov A. Y., Lidstrom M. E. 1995; Cloning, sequencing and mutation of a gene for azurin in Methylobacillus flagellatum KT. J Bacteriol 177:4575–4578
    [Google Scholar]
  12. Gak E. R., Tsygankov Y. D., Chistoserdov A. Y. 1997; Organization of methylamine utilization genes ( mau ) from ‘ Methylobacillus flagellatum ’ KT: cloning and analysis of mutants. Microbiology 143:1827–1835 [CrossRef]
    [Google Scholar]
  13. Govindaraj S., Eisenstein E., Jones L. H., Sanders-Loehr J., Chistoserdov A. Y., Davidson V. L., Edwards S. L. 1994; Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. J Bacteriol 176:2922–2929
    [Google Scholar]
  14. Graichen M. E., Jones L. H., Sharma B. V., Holster J. P., Davidson V. L., van Spanning R. J. M. 1999; Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides . J Bacteriol 181:4216–4222
    [Google Scholar]
  15. Haywood G. W., Janschke N. S., Large P. J., Wallis J. M. 1982; Properties and subunit structure of methylamine dehydrogenase from Thiobacillus A2 and Methylophilus methylotrophus . FEMS Microbiol Lett 15:79–82 [CrossRef]
    [Google Scholar]
  16. Huitema F., Van Beeumen J., Van Driessche G., Duine J. A., Canters G. W. 1993; Cloning and sequencing of the gene coding for the large subunit of methylamine dehydrogenase from Thiobacillus versutus . J Bacteriol 175:6254–6259
    [Google Scholar]
  17. Husain M., Davidson V. L. 1987; Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans . J Bacteriol 169:1712–1717
    [Google Scholar]
  18. Iwaki M., Yagi T., Horiike K., Saeki Y., Ushijima T., Nozaki M. 1983; Crystallization and properties of aromatic amine dehydrogenase from Pseudomonas sp. Arch Biochem Biophys 220:253–262 [CrossRef]
    [Google Scholar]
  19. Katayama Y., Hiraishi A., Kuraishi H. 1995; Paracoccus thiocyanatus sp. nov., a new species of thiocyanate-utilizing facultative chemolithotroph, and transfer of Thiobacillus versutus to the genus Paracoccus as Paracoccus versutus comb. nov. with emendation of the genus. Microbiology 141:1469–1477 [CrossRef]
    [Google Scholar]
  20. Kenny W. C., McIntire W. 1983; Characterization of methylamine dehydrogenase from bacterium W3A1: interaction with reductant and amino-containing compounds. Biochemistry 22:3858–3868 [CrossRef]
    [Google Scholar]
  21. Kirukhin M. Y., Chistoserdov A. Y., Tsygankov Y. D. 1990; Methylamine dehydrogenase from Methylobacillus flagellatum . Methods Enzymol 188:247
    [Google Scholar]
  22. Lawrence J. G., Roth J. R. 1996; Selfish operons: horizontal transfer may drive the evolution of gene clusters. Genetics 143:1843–1860
    [Google Scholar]
  23. Lidstrom M. E., Chistoserdov A. Y. 1993; Molecular biology and genetics of methylamine dehydrogenases. In Microbial Growth on C1 Compounds pp 381–400 Edited by Murrell J. C., Kelly D. P. Andover: Intercept;
    [Google Scholar]
  24. McIntire W. S., Hartmann C. 1992; Copper-containing amine oxidases. In Principles and Applications of Quinoproteins pp 97–172 Edited by Davidson V. New York: Marcel Dekker;
    [Google Scholar]
  25. McIntire W. S., Wemmer D. E., Chistoserdov A. Y., Lidstrom M. E. 1991; A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase. Science 25:817–824
    [Google Scholar]
  26. Maniatis T., Fritsch E. F., Sambrook J. 1982 Molecular Cloning: a Laboratory Manual Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  27. Marmur J. 1961; A procedure for the isolation of deoxyribonucleic acid from microorganisms. J Mol Biol 3:208–218 [CrossRef]
    [Google Scholar]
  28. Matsumoto T. 1978; Methylamine dehydrogenase of Pseudomonas sp. J: purification and properties of the subunits. Biochim Biophys Acta 522:291–302 [CrossRef]
    [Google Scholar]
  29. Nozaki M. 1987; Aromatic amine dehydrogenase from Alcaligenes faecalis . Methods Enzymol 142:650–655
    [Google Scholar]
  30. Owens J. D., Keddie R. M. 1969; The nitrogen nutrition of soil and herbage coryneform bacteria. J Appl Bacteriol 32:338–347 [CrossRef]
    [Google Scholar]
  31. Ruvkun G. B., Ausubel F. M. 1981; A general method for site-directed mutagenesis in prokaryotes. Nature 289:85–88 [CrossRef]
    [Google Scholar]
  32. Simon R. 1984; High-frequency mobilization of Gram-negative bacterial replicons by the in vitro constructed Tn 5 - mob transposon. Mol Gen Genet 196:413–420 [CrossRef]
    [Google Scholar]
  33. Taguchi K., Kudo T., Tobari J. 1997; Genetic organization and characterization of the mau gene cluster, which concerned the intial step of electron transfer chains involved in methylamine oxidation of the obligate methylotroph Methylomonas sp. strain J. . J Ferment Bioeng 84:502–510 [CrossRef]
    [Google Scholar]
  34. Tarr H. L. A. 1954; Microbial deterioration of fish post mortem , its detection and control. Bacteriol Rev 15:1–15
    [Google Scholar]
  35. Titani K., Ericsson L. H., Hon-Nami K., Miyazawa T. 1985; Amino acid sequence of cytochrome c 552 from Thermus thermophilus . Biochem Biophys Res Commun 128:781–787 [CrossRef]
    [Google Scholar]
  36. Ubbink M., van Kleef M. A. G., Kleinjan D.-J., Hoitink C. W. G., Huitema F., Beintema J. J., Duine J. A., Canters G. W. 1991; Cloning, sequencing and expression studies of the genes encoding amicyanin and the β-subunit of methylamine dehydrogenase from Thiobacillus versutus. Eur J Biochem 202:1003–1012 [CrossRef]
    [Google Scholar]
  37. Van der Palen C. J. N. M., Slotboom D. J., Jongejan L., Reijnders W. N. M., Harms N., Duine J. A., Van Spanning R. J. M. 1995; Mutational analysis of mau genes involved in methylamine metabolism in Paracoccus denitrificans . Eur J Biochem 230:860–871 [CrossRef]
    [Google Scholar]
  38. Van der Palen C. J. N. M., Reijnders W. N. M., Duine J. A., de Vries S., van Spanning R. J. M. 1997; MauE and MauD proteins are essential in methylamine metabolism of Paracoccus denitrificans . Antonie Leeuwenhoek 72:219–228 [CrossRef]
    [Google Scholar]
  39. Van Neste A., Duce R. A., Lee C. 1987; Methylamines in the marine atmosphere. Geophys Res Lett 14:711–714 [CrossRef]
    [Google Scholar]
  40. Van Spanning R. J. M., Wansell C. W., Reijnders W. N. M., Oltman L. F., Stouthamer A. H. 1990; Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation. FEBS Lett 275:217–220 [CrossRef]
    [Google Scholar]
  41. Whitaker J. R., Granum P. E. 1980; An absolute method for protein determination based on difference in absorbance at 235 and 280 nm. Anal Biochem 109:156–159 [CrossRef]
    [Google Scholar]
  42. Zhu A., Sun D., Davidson V. L. 1999; Localization of periplasmic redox proteins of Alcaligenes faecalis by a modified general method for fractionating Gram-negative bacteria. J Bacteriol 181:6540–6542
    [Google Scholar]
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