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Original Articles

Cloning and Enhanced Expression of the Cytochrome P450nor Gene (nicA; CYP55A5) Encoding Nitric Oxide Reductase from Aspergillus oryzae

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Pages 2040-2049 | Received 08 Mar 2004, Accepted 29 Jul 2004, Published online: 22 May 2014

  • 1) Yamanaka, T., “The Biochemistry of Bacterial Cytochromes”, Japan Scientific Societies Press and Springer-Verlag, Tokyo and Berlin, pp. 3–15 (1992).
  • 2) Coyne, M. S., Arunakumari, A., Averill, B. A., and Tiedje, J. M., Immunological identification and distribution of dissimilatory heme cd1 and nonheme copper nitrite reductases in denitrifying bacteria. Appl. Environ. Microbiol., 55, 2924–2931 (1989).
  • 3) Ferguson, S. J., Denitrification: a question of the control and organization of electron and ion transport. Trends Biochem. Sci., 12, 354–357 (1987).
  • 4) Knowles, R., Denitrification. Microbiol. Rev., 46, 43–70 (1982).
  • 5) Shoun, H., and Tanimoto, T., Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction. J. Biol. Chem., 266, 11078–11082 (1991).
  • 6) Shoun, H., Kim, D. H., Uchiyama, H., and Sugiyama, J., Denitrification by fungi. FEMS Microbiol. Lett., 73, 277–281 (1992).
  • 7) Usuda, K., Toritsuka, N., Matsuo, Y., Kim, D. H., and Shoun, H., Denitrification by the fungus Cylindrocarpon tonkinense: anaerobic cell growth and two isozyme forms of cytochrome P-450nor. Appl. Environ. Microbiol., 61, 883–889 (1995).
  • 8) Tsuruta, S., Takaya, N., Zhang, L., Shoun, H., Kimura, K., Hamamoto, M., and Nakase, T., Denitrification by yeasts and occurrence of cytochrome P450nor in Trichosporon cutaneum. FEMS Microbiol. Lett., 168, 105–110 (1998).
  • 9) Kizawa, H., Tomura, D., Oda, M., Fukamizu, A., Hoshino, T., Gotoh, O., Yasui, T., and Shoun, H., Nucleotide sequence of the unique nitrate/nitrite-inducible cytochrome P-450 cDNA from Fusarium oxysporum. J. Biol. Chem., 266, 10632–10637 (1991).
  • 10) Park, S. Y., Shimizu, H., Adachi, S., Nakagawa, A., Tanaka, I., Nakahara, K., Shoun, H., Obayashi, E., Nakamura, H., Iizuka, T., and Shiro, Y., Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum. Nat. Struct. Biol., 10, 827–832 (1997).
  • 11) Kudo, T., Tomura, D., Liu, D. L., Dai, X. Q., and Shoun, H., Two isozymes of P450nor of Cylindrocarpon tonkinense: molecular cloning of the cDNAs and genes, expressions in the yeast, and the putative NAD(P)H-binding site. Biochimie, 78, 792–799 (1996).
  • 12) Zhang, L., Takaya, N., Kitazume, T., Kondo, T., and Shoun, H., Purification and cDNA cloning of nitric oxide reductase cytochrome P450nor (CYP55A4) from Trichosporon cutaneum. Eur. J. Biochem., 268, 3198–3204 (2001).
  • 13) Shoun, H., Sudo, Y., Seto, Y., and Beppu, T., Purification and properties of a cytochrome P-450 of a fungus, Fusarium oxysporum. J. Biochem. (Tokyo), 94, 1219–1229 (1983).
  • 14) Nakahara, K., and Shoun, H., N-terminal processing and amino acid sequence of two isoforms of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum. J. Biochem. (Tokyo), 120, 1082–1087 (1996).
  • 15) Nakahara, K., Tanimoto, T., Hatano, K., Usuda, K., and Shoun, H., Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor. J. Biol. Chem., 268, 8350–8355 (1993).
  • 16) Tomura, D., Obika, K., Fukamizu, A., and Shoun, H., Nitric oxide reductase cytochrome P-450 gene, CYP 55, of the fungus Fusarium oxysporum containing a potential binding-site for FNR, the transcription factor involved in the regulation of anaerobic growth of Escherichia coli. J. Biochem. (Tokyo), 116, 88–94 (1994).
  • 17) Unkles, S. E., Campbell, E. I., Ruiter-Jacobs, Y. M. J. T., Broekhuijsen, M., Macro, J. A., Carrez, D., Contreras, R., Hondel, C. A. M. J. J., and Kinghorn, J. R., The development of a homologous transformation system for Aspergillus oryzae based on the nitrate assimilation pathway: a convenient and general selection system for filamentous fungal transformation. Mol. Gen. Genet., 218, 99–104 (1989).
  • 18) Hanahan, D., Studies on the transformation of Escherichia coli with plasmids. J. Mol. Biol., 166, 557–580 (1983).
  • 19) Gomi, K., Iimura, Y., and Hara, S., Integrative transformation of Aspergillus oryzae with a plasmid containing the Aspergillus nidulans argB gene. Agric. Biol. Chem., 51, 2549–2555 (1987).
  • 20) Kitamoto, N., Kimura, T., Kito, Y., Ohmiya, K., and Tsukagoshi, N., The nitrate reductase gene from a shoyu koji mold, Aspergillus oryzae KBN616. Biosci. Biotechnol. Biochem., 59, 1795–1797 (1995).
  • 21) Ishida, H., Hata, Y., Ichikawa, E., Kawato, A., Suginami, K., and Imayasu, S., Regulation of the glucoamysale-encoding gene (glaB) expressed in solid-state culture (koji) of Aspergillus oryzae. J. Ferment. Bioeng., 86, 301–307 (1998).
  • 22) Ishida, H., Matsumura, K., Hata, Y., Kawato, A., Suginami, K., Abe, Y., Imayasu, S., and Ichishima, E., Establishment of a hyper-protein production system in submerged Aspergillus oryzae culture under tyrosinase-encoding gene (melO) promoter control. Appl. Microbiol. Biotechnol., 57, 131–137 (2001).
  • 23) Jefferson, R. A., Burgess, S. M., and Hirsh, D., β-Glucuronidase from Escherichia coli as a gene-fusion marker. Proc. Natl. Acad. Sci. U.S.A., 83, 8447–8451 (1986).
  • 24) Omura, T., and Sato, R., The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties. J. Biol. Chem., 239, 2379–2385 (1964).
  • 25) Punt, P. J., Strauss, J., Smit, R., Kinghorn, J. R., van den Hondel, C. A., and Scazzocchio, C., The intergenic region between the divergently transcribed niiA and niaD genes of Aspergillus nidulans contains multiple NirA binding sites which act bidirectionally. Mol. Cell. Biol., 15, 5688–5699 (1995).
  • 26) Kato, M., Studies on assembly mechanisms and transcriptional enhancing activity of the CCAAT-box binding complex in Aspergillus oryzae. Nippon Nogeikagaku Kaishi (in Japanese), 77, 960–967 (2003).
  • 27) Takaya, N., Uchimura, H., Lai, Y., and Shoun, H., Transcriptional control of nitric oxide reductase gene (CYP55) in the fungal denitrifier Fusarium oxysporum. Biosci. Biotechnol. Biochem., 66, 1039–1045 (2002).
  • 28) Zhang, L., Kudo, T., Takaya, N., and Shoun, H., The B′ helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH. J. Biol. Chem., 277, 33842–33847 (2002).
  • 29) Yoshida, M., Akaike, T., Wada, Y., Sato, K., Ikeda, K., Ueda, S., and Maeda, H., Therapeutic effects of imidazolineoxyl N-oxide against endotoxin shock through its direct nitric oxide-scavenging activity. Biochem. Biophys. Res. Commun., 202, 923–930 (1994).
  • 30) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685 (1970).

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