Expression in<i>Escherichia coli</i>of Biphenyl 2,3-Dioxygenase Genes from a Gram-Positive Polychlorinated Biphenyl Degrader,<i>Rhodococcus jostii</i>RHA1

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  • OHMORI Tsuneo
    Department of Bioengineering, Nagaoka University of Technology
  • MORITA Hirokazu
    Department of Bioengineering, Nagaoka University of Technology
  • TANAKA Megumi
    Department of Bioengineering, Nagaoka University of Technology
  • TOMOI Masanori
    Department of Bioengineering, Nagaoka University of Technology
  • MIYAUCHI Keisuke
    Department of Civil and Environmental Engineering, Tohoku Gakuin University
  • KASAI Daisuke
    Department of Bioengineering, Nagaoka University of Technology
  • FURUKAWA Kensuke
    Department of Food and Bioscience, Faculty of Food Science and Nutrition, Beppu University
  • MASAI Eiji
    Department of Bioengineering, Nagaoka University of Technology
  • FUKUDA Masao
    Department of Bioengineering, Nagaoka University of Technology

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  • Expression in Escherichia coli of Biphenyl 2,3-Dioxygenase Genes from a Gram-Positive Polychlorinated Biphenyl Degrader, Rhodococcus jostii RHA1

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Rhodococcus jostii RHA1 is a polychlorinated biphenyl degrader. Multi-component biphenyl 2,3-dioxygenase (BphA) genes of RHA1 encode large and small subunits of oxygenase component and ferredoxin and reductase components. They did not express enzyme activity in Escherichia coli. To obtain BphA activity in E. coli, hybrid BphA gene derivatives were constructed by replacing ferredoxin and/or reductase component genes of RHA1 with those of Pseudomonas pseudoalcaligenes KF707. The results obtained indicate a lack of catalytic activity of the RHA1 ferredoxin component gene, bphAc in E. coli. To determine the cause of inability of RHA1 bphAc to express in E. coli, the bphAc gene was introduced into Rosetta (DE3) pLacI, which has extra tRNA genes for rare codons in E. coli. The resulting strain abundantly produced the bphAc product, and showed activity. These results suggest that codon usage bias is involved in inability of RHA1 bphAc to express its catalytic activity in E. coli.

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