Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri

Journal of Biochemistry

Volumn 120, Issue 4, 1996, Pages 736-744

  Zenno, Shuhei ^a,c   Koike, Hideaki ^b   Tanokura, Masaru ^b   Saigo, Kaoru ^a  

^a Graduate School of Science   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c CHISSO CORPORATION   (Japan)

Author keywords

Escherichia coli; Flavin reductase; Flavoenzyme; nfsB; Nitroreductase

Indexed keywords

FLAVOPROTEIN; NITROREDUCTASE;

AMINO ACID SEQUENCE; ARTICLE; ENERGY METABOLISM; ENTEROBACTER CLOACAE; ESCHERICHIA COLI; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; POLYMERASE CHAIN REACTION; SALMONELLA; VIBRIO;

ENTEROBACTER CLOACAE; ESCHERICHIA COLI; SALMONELLA; SALMONELLA TYPHIMURIUM; TYPHIMURIUM; VIBRIO; VIBRIO FISCHERI;

EID: 0029808844     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021473     Document Type: Article

References (45)

1. Zenno, S., Saigo, K., Kanoh, H., and Inouye, S. (1994) Identification of the gene encoding the major NAD(P)H-flavin oxidoreductase of the bioluminescent bacteria Vibrio fiacheri ATCC 7744. J. Bacterial. 176, 3536-3543
2. Watanabe, M., Ishidate, M., Jr., and Nohmi, T. (1990) Nucleotide sequence of Salmonella typhimurium nitroreductase gene. Nucleic Acids Res. 18, 1059
3. Bryant, C., Hubbard, L., and McElroy, W.D. (1991) Cloning, nucleotide sequence, and expression of the nitroreductase gene from Enterobacter cloacae. J. Biol. Chem. 266, 4126-4130
4. Zenno, S. and Saigo, K. (1994) Identification of the genes encoding NAD(P)H-flavin oxidoreductases, similar in sequence to Escherichia coli Fre, in 4 species of luminous bacteria, Photorhabdus luminescens, Vibrio fischeri, Vibrio harveyi and Vibrio orientalis. J. Bacterial. 176, 3544-3551
5. Fontecave, M., Eliasson, R., and Reichard, P. (1987) NAD(P)H: flavin oxidoreductase of Escherichia coli: A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase. J. Biol. Chem. 262, 12325-12331
6. Spyrou, G., Haggard-Ljungquist, E., Krook, M., Jornvall, H., Nilsson, E., and Reichard, P. (1991) Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme. J. Bacterial. 173, 3673-3679
7. Asnis, R.E. (1957) The reduction of furacin by cell-free extracts of furacin-resistant and parent-susceptible strains of Escherichia coli. Arch. Biochem. Biophys. 66, 208-216
8. McCalla, D.R., Reuvers, A., and Kaiser, C. (1970) Mode of action of nitrofurazone, J. Bacterial. 104, 1126-1134
9. Watanabe, M., Ishidate, M., Jr., and Nohmi, T. (1989) A sensitive method for the detection of mutagenic nitroarenes: Construction of nitroreductase-overproducing derivatives of Salmonella typhimurium TA98 and TA100. Mutat. Res. 216, 211-220
10. Bryant, C. and DeLuca, M. (1991) Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae. J. Biol. Chem. 266, 4119-4125
11. Bryant, D.W., McCalla, D.R., Leeksma, M., and Laneuville, P. (1981) Type I nitroreductases of Eacherichia coli. Can. J. Microbiol. 27, 81-86
12. McCalla, D.R., Kaiser, C., and Green, M.H.L. (1978) Genetics of nitrofurazone resistance in Escherichia coli. J. Bacterial. 133, 10-16
13. Zenno, S., Koike, H., Tanokura, M., and Saigo, K. (1996) Conversion of NfsB, a minor Escherichia coli nitroreductase, to a flavin reductase similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri, by a single amino acid substitution. J. Bacterial. 178, 4731-4733
14. Appleyard, R.K. (1954) Segregation of lambda lysogenicity during bacterial recombination in E. coli K-12. Genetics 39, 429-439
15. Raleigh, E. and Wilson, G. (1986) Escherichia coli K-12 restricts DNA containing 5-methylcytosine. Proc. Natl. Acad. Sci. USA 83, 9070-9074
16. de Boer, H.A., Comstock, L.J., and Vasser, M. (1983) The tac promoter: A functional hybrid derived from the trp and lac promoters. Proc. Natl. Acad. Sci. USA 80, 21-25
17. Messing, J. and Vieira, J. (1982) A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments. Gene 19, 269-276
18. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
19. Messing, J. (1983) New M13 vectors for cloning. Methods Enzymol. 101, 20-78
20. Vieira, J. and Messing, J. (1987) Production of single-stranded plasmid DNA. Methods Emymol. 153, 3-11
21. Saiki, R.K., Gelfand, D.H., Stoffel, S., Scharf, S.J., Higuchi, R., Horn, G.T., Mullis, K.B., and Erlich, H.A. (1988) Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science 239, 487-491
22. Kohara, Y., Akiyama, K., and Isono, K. (1987) The physical map of whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50, 495-508
23. Chung, C.T., Niemela, S.L., and Miller, R.H. (1989) One-step preparation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution. Proc. Natl. Acad. Sci. USA 86, 2172-2175
24. Inouye, S., Zenno, S., Sakaki, Y., and Tsuji, F.I. (1991) High-level expression and purification of apoaequorin. Protein Exp. Purif. 2, 122-126
25. 5 reductase. J. Biol. Chem. 236, 2329-2335
26. Brew, K., Shaper, J.H., Olsen, K.W., Trayer, I.P., and Hill, R.L. (1975) Cross-linking of the components of lactose synthetase with dimethylpimelimidate. J. Biol. Chem. 250, 1434-1444
27. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
28. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685
29. Ohnishi, K., Niimura, Y., Yokoyama, K., Hidaka, M., Masaki, H., Uchimura, T., Suzuki, H., Uozumi, T., Kozaki, M., Komagata, K., and Nishino, T. (1994) Purification and analysis of a flavoprotein functional as NADH oxidase from Amphibacillus xylanus overexpressed in Escherichia coli. J. Biol. Chem. 269, 31418-31423
30. Feinberg, A.P. and Vogelstein, B. (1983) A technique for radio-labeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132, 6-13
31. Hattori, M. and Sakaki, Y. (1988) Dideoxy sequencing method using denatured plasmid templates. Anal. Biochem. 152, 232-238
32. Uemori, T., Ishino, Y., Fujita, K., Asada, K., and Kato, I. (1993) Cloning of the DNA polymerase gene of Bacillus caldotenax and characterization of the gene product. J. Biochem. 113, 401-410
33. 2-forming NADH oxidase from the extreme thermophilic Thermos thermophilus HB8 and its expression in Escherichia coli. Eur. J. Biochem. 205, 875-679; (1993) Corrections 211, 909
34. Park, H.-J., Reiser, C.O.A., Kondruweit, S., Erdmann, H., Schmid, R.D., and Sprinzl, M. (1992) Purification and characterization of a NADH oxidase from the thermophile Thermus thermophilus HB8. Eur. J. Biochem. 205, 881-885
35. Fleischmann, R.D., Adams, M.D., White, O., Clayton, R.A., Kirkness, E.F., Kerlavage, A.R., Bult, C.J., Tomb, J.-F., Dougherty, B.A., Merrick, J.M., McKenney, K., Sutton, G., FitzHugh, W., Fields, C., Gocayne, J.D., Scott, J., Shirley, R., Liu, L.-I., Glodek, A., Kelley, J.M., Weidman, J.F., Phillips, C.A., Spriggs, T., Hedblom, E., Cotton, M.D., Utterback, R.C., Hanna, M.C., Nguyen, D.T., Saudek, D.M., Brandon, R.C., Fine, L.D., Fritchman, J.L., Fuhrmann, J.L., Geoghagen, N.S.M., Gnehm, C.L., McDonald, L.A., Small, K.V., Fraser, C.M., Smith, H.O., and Venter, J.C. (1995) Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269, 496-512
36. Bachmann, B.J. (1990) Linkage map of Escherichia coli K-12, edition 8. Microbiol. Rev. 54, 130-197
37. Inouye, S. (1994) NAD(P)H-flavin oxidoreductase from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, is a flavoprotein. FEBS Lett. 347, 163-168
38. Tu, S.-C., Becvar, J.E., and Hastings, J.W. (1979) Kinetic studies on the mechanism of bacterial NAD(P)H:flavin oxidoreductase. Arch. Biochem. Biophys. 193, 110-116
39. Zenno, S., Koike, H., Kumar, A.N., Jayaraman, R., Tanokura, M., and Saigo, K. (1996) Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase. J. Bacterial. 178, 4508-4514
40. Michael, N.P., Brehm, J.K., Anlezark, G.M., and Minton, N.P. (1994) Physical characterization of the Escherichia coli B gene encoding nitroreductase and its over-expression in Escherichia coli K12. FEMS Microbiol. Lett. 124, 195-202
41. Ghisla, S. and Massey, V. (1989) Mechanisms of flavoprotein-catalyzed reactions. Eur. J. Biochem. 181, 1-17
42. Hecht, H.J., Erdmann, H., Park, H.J., Sprinzl, M., and Schmid, R.D. (1995) Crystal structure of NADH oxidase from Thermus thermophilus. Nature Struct. Biol. 2, 1109-1114
43. Rosenberg, M. and Court, D. (1979) Regulatory sequences involved in the promotion and termination of RNA transcription. Annu. Rev. Genet. 13, 319-353
44. Shine, J. and Dalgarno, L. (1974) The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 71, 1342-1346
45. Schwartz, R.M. and Dayhoff, M.O. (1978) Matrices for detecting distant relationships in Atlas of Protein Sequence and Structure (Dayhoff, M.O., ed.) Vol. 5, Supplement 3, pp. 353-358, National Biochemical Research Foundation, Washington, DC