NahW, a novel, inducible salicylate hydroxylase involved in mineralization of naphthalene by Pseudomonas stutzeri AN10

Journal of Bacteriology

Volumn 181, Issue 8, 1999, Pages 2315-2322

  Bosch, Rafael ^a,b   Moore, Edward R B ^b   García Valdés, Elena ^a   Pieper, Dietmar H ^b  

^a UNIVERSITAT DE LES ILLES BALEARS   (Spain)

^b HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

NAPHTHALENE; OXYGENASE; SALICYLIC ACID;

ARTICLE; BACTERIAL GENE; BACTERIAL METABOLISM; GENE LOCATION; MINERALIZATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PSEUDOMONAS STUTZERI;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA; PROKARYOTA; PSEUDOMONAS; PSEUDOMONAS STUTZERI;

EID: 0032960144     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.8.2315-2322.1999     Document Type: Article

References (54)

1. Amengual, J. F. 1992. Metabolismo de derivados halogenados y metilados del naftaleno por Pseudomonas stutzeri AN10. Ph.D. thesis. Universitat de les Illes Balears, Palma de Mallorca, Spain.
2. Aragno, M., and H. G. Schlegel. 1981. The hydrogen-oxidizing bacteria, p. 865-893. In M. P. Starr, et al. (ed.), The prokaryotes. A handbook on habitats, isolation, and identification of bacteria. Springer-Verlag, Berlin and Heildelberg, Germany.
3. Barnsley, E. A. 1975. The induction of enzymes of naphthalene metabolism in pseudomonads by salicylate and 2-aminobenzoate. J. Gen. Microbiol. 88:193-196.
4. Bosch, R., E. García-Valdés, and E. R. B. Moore. Complete nucleotide sequence and evolutionary significance of a chromosomally encoded naphthalene-degradation pathway from Pseudomonas stutzeri AN10. Submitted for publication.
5. Cairns, J., J. Overbaugh, and S. Miller. 1988. The origin of mutants. Nature 335:142-145.
6. Cane, P. A., and P. A. Williams. 1986. A restriction map of naphthalene catabolic plasmid pWW60-1 and the location of some of its catabolic genes. J. Gen. Microbiol. 132:2919-2929.
7. Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
8. Dhaese, P., H. De Greve, H. Decraemer, J. Schell, and M. Van Mongatu. 1979. Rapid mapping of transposon insertion and deletion mutations in the large Ti-plasmids of Agrobacterium tumefaciens. Nucleic Acids Res. 7:1837-1849.
9. Eggink, G., H. Engel, G. Vriend, P. Terpstra, and B. Witholt. 1990. Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints. J. Mol. Biol. 212:135-142.
10. Einarsdottir, G. H., M. T. Stankovich, and S.-C. Tu. 1988. Studies of electron transfer properties of salicylate hydroxylase from Pseudomonas cepacia and effects of salicylate and benzoate binding. Biochemistry 27:3277-3285.
11. Fujita, M., S. Hashimoto, M. Takeo, and K. Hagino. 1989. Plasmid-coded degradation of salicylate using the catechol cleavage pathway of the host. J. Ferment. Bioeng. 67:286-290.
12. Ginard, M., U. Römling, B. Tümmler, and J. Lalucat. 1996. Naphthalene degradation is chromosomally encoded in Pseudomonas stutzeri, p. 183. In Abstracts of 1996 Biodegradation of Organic Pollutants Symposium. Palma de Mallorca, Spain.
13. Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
14. Harayama, S., M. Kok, and E. L. Neidle. 1992. Functional and evolutionary relationships among diverse oxygenases. Annu. Rev. Microbiol. 46:565-601.
15. Harayama, S., M. Rekik, A. Wasserfallen, and A. Bairoch. 1987. Evolutionary relationships between catabolic pathways for aromatics: conservation of gene order and nucleotide sequences of catechol oxidation genes of pWWO and NAH7 plasmids. Mol. Gen. Genet. 210:241-247.
16. Harayama, S., and K. N. Timmis. 1992. Aerobic biodegradation of aromatic hydrocarbons by bacteria, p. 99-156. In H. Sigel and A. Sigel (ed.), Degradation of environmental pollutants by microorganisms and their metalloenzymes. Marcel Dekker Inc., New York, N.Y.
17. Harlow, E., and E. Lane. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
18. Kasak, L., R. Horak, A. Nurk, K. Talvik, and M. Kivisaar. 1993. Regulation of the catechol 1,2-dioxygenase-and phenol monooxygenase-encoding pheBA operon in Pseudomonas putida PaW85. J. Bacteriol. 175:8038-8042.
19. Kröger, M., and G. Hobom. 1982. Structural analysis of insertion sequence IS5. Nature 297:159-162.
20. Lee, J., J. Oh, K. R. Min, and Y. Kim. 1996. Nucleotide sequence of salicylate hydroxylase gene and its 5′-flanking region of Pseudomonas putida KF715. Biochem. Biophys. Res. Commun. 218:544-548.
21. Lehrbach, P. R., J. Zeyer, W. Reineke, H.-J. Knackmuss, and K. N. Timmis. 1984. Enzyme recruitment in vitro: use of cloned genes to extend the range of haloaromatics degraded by Pseudomonas sp. strain B13. J. Bacteriol. 158:1025-1032.
22. Morris, C. M., and E. A. Barnsley. 1982. The cometabolism of 1-and 2-chloronaphthalene by pseudomonads. Can. J. Microbiol. 28:73-79.
23. Platt, A., V. Shingler, S. C. Taylor, and P. A. Williams. 1995. The 4-hydroxy-2-oxovalerate aldolase and acetaldehyde dehydrogenase (acylating) encoded by the nahM and nahO genes of the naphthalene catabolic plasmid pWW60-22 provide further evidence of conservation of meta-cleavage pathway gene sequences. Microbiology 141:2223-2233.
24. Rossello, R., E. García-Valdés, J. Lalucat, and J. Ursing. 1991. Genotypic and phenotypic diversity of Pseudomonas stutzeri. Syst. Appl. Microbiol. 14:150-157.
25. Rosselló-Mora, R. A., J. Lalucat, and E. García-Valdés. 1994. Comparative biochemical and genetic analysis of naphthalene degradation among Pseudomonas stutzeri strains. Appl. Environ. Microbiol. 60:966-972.
26. Roth, J. R., N. Benson, T. Galitski, K. Haack, J. G. Lawrence, and L. Miesel. 1996. Rearrangements of the bacterial chromosome: formation and applications, p. 2256-2276. In F. C. Neidhardt, et al. (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. 2. ASM Press, Washington, D.C.
27. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
28. Schell, M. A. 1985. Transcriptional control of the nah and sal hydrocarbon-degradation operons by the nahR gene product. Gene 36:301-309.
29. Schell, M. A., and P. E. Wender. 1986. Identification of the nahR gene product and nucleotide sequences required for its activation of the sal operon. J. Bacteriol. 166:9-14.
30. Simon, M. J., T. D. Osslund, R. Saunders, B. D. Ensley, S. Suggs, A. Harcourt, W. Suen, D. L. Cruden, D. T. Gibson, and G. J. Zylstra. 1993. Sequences of genes encoding naphthalene dioxygenase in Pseudomonas putida strains G7 and NCIB9816-4. Gene 127:31-37.
31. Smith, P. K., R. I. Krohn, G. T. Hermanson, A. K. Mallia, F. H. Gartner, M. D. Provenzano, E. K. Fujimoto, N. M. Goeke, B. J. Olson, and D. C. Klenk. 1985. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150:76-85.
32. Suzuki, K., and M. Katagiri. 1981. Mechanism of salicylate hydroxylase-catalyzed decarboxylation. Biochim. Biophys. Acta 657:530-534.
33. Suzuki, K., M. Mizuguchi, T. Gomi, and E. Itagaki. 1995. Identification of a lysine residue in the NADH-binding site of salicylate hydroxylase from Pseudomonas putida S-1. J. Biochem. 117:579-585.
34. Suzuki, K,. M. Mizuguchi, K. Ohnishi, and E. Itagaki. 1996. Structure of chromosomal DNA coding for Pseudomonas putida S-1 salicylate hydroxylase. Biochim. Biophys. Acta 1275:154-156.
35. Suzuki, K., and K. Ohnishi. 1990. Functional modification of an arginine residue on salicylate hydroxylase. Biochim. Biophys. Acta 1040:327-336.
36. Suzuki, K., S. Takemori, and M. Katagiri. 1969. Mechanism of the salicylate hydroxylase reaction. IV. Fluorometric analysis of the complex formation. Biochim. Biophys. Acta 191:77-85.
37. Takemori, S, K. Hon-nami, F. Kawahara, and M. Katahiri. 1974. Mechanism of the salicylate hydroxylase reaction. VI. The monomeric nature of the enzyme. Biochim. Biophys. Acta 342:137-144.
38. Takemori, S., M. Nakamura, K. Suzuki, M. Katagiri, and T. Nakamura. 1972. Mechanism of salicylate hydroxylase reaction. V. Kinetic analyses. Biochim. Biophys. Acta 284:382-393.
39. Takemori, S., H. Yasuda, K. Mihara, K. Suzuki, and M. Katagiri. 1969. Mechanism of the salicylate hydroxylase reaction. II. The enzyme-substrate complex. Biochim. Biophys. Acta 191:58-68.
40. Takemori, S., H. Yasuda, K. Mihara, K. Suzuki, and M. Katagiri. 1969. Mechanism of the salicylate hydroxylase reaction. III. Characterization and reactivity of chemically or photochemically reduced enzyme-flavin. Biochim. Biophys. Acta 191:69-76.
41. Tsuji, H., T. Oka, M. Kimoto, Y. M. Hong, Y. Natori, and T. Ogawa. 1996 Cloning and sequencing of cDNA encoding 4-aminobenzoate hydroxylase from Agaricus bisporus. Biochim. Biophys. Acta 1309:31-36.
42. Tu, S.-C., F. A. Romero, and L.-H. Wang. 1981. Uncoupling of the substrate monooxygenation and reduced pyridine nucleotide oxidation activities of salicylate hydroxylase by flavins. Arch. Biochem. Biophys. 209:423-432.
43. Wang, L.-H., and S.-C. Tu. 1984. The kinetic mechanism of salicylate hydroxylase as studied by initial rate measurement, rapid reaction kinetics, and isotope effects. J. Biol. Chem. 259:10682-10688.
44. Wang, L.-H, S.-C. Tu, and R. C. Lusk. 1984. Apoenzyme of Pseudomonas cepacia salicylate hydroxylase. Preparation, fluorescence property, and nature of flavin binding. J. Biol. Chem. 259:1136-1142.
45. Weijer, W. J., J. Hofsteenge, J. M. Vereijken, P. A. Jekel, and J. J. Beintema. 1982. Primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Biochim. Biophys. Acta 704:385-388.
46. While-Stevens, R. H., and H. Kamin. 1972. Studies of a flavoprotein, salicylate hydroxylase. I. Preparation, properties, and the uncoupling of oxygen reduction from hydroxylation. J. Biol. Chem. 247:2358-2370.
47. White-Stevens, R. H., H. Kamin, and Q. H. Gibson. 1972. Studies of a flavoprotein, salicylate hydroxylase. H. Enzyme mechanism. J. Biol. Chem. 247:2371-2381.
48. αβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187:101-107.
49. Williams, P. A., and J. R. Sayers. 1994. The evolution of pathways for aromatic hydrocarbon oxidation in Pseudomonas. Biodegradation 5:195-217.
50. Yamamoto, S., M. Katagiri, H. Maeno, and O. Hayaishi. 1965. Salicylate hydroxylase, a monooxygenase requiring flavin adenine dinucleotide. I. Purification and general properties. J. Biol. Chem. 240:3408-3413.
51. Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
52. Yen, K., and I. C. Gunsalus. 1982. Plasmid gene organization: naphthalene/salicylate oxidation. Proc. Natl. Acad. Sci. USA 79:874-878.
53. You, I., D. Ghosal, and I. C. Gunsalus. 1991. Nucleotide sequence analysis of the Pseudomonas putida PpG7 salicylate hydroxylase gene (nahG) and its 3′-flanking region. Biochemistry 30:1635-1641.
54. You, I.-S., R. I. Murray, D. Jollic, and I. C. Gunsalus. 1990. Purification and characterization of salicylate hydroxylase from Pseudomonas putida PpG7. Biochem. Biophys. Res. Commun. 169:1049-1054.