Identification of the novel <i>hcbB</i> operon catalyzing the dechlorination of pentachlorophenol in the Gram-positive bacterium <i>Nocardioides</i> sp. strain PD653

  • Ito Koji
    Department of Agricultural Chemistry, Tokyo University of Agriculture Hazardous Chemicals Division, Institute for Agro-Environmental Sciences, NARO
  • Takagi Kazuhiro
    Department of Agricultural Chemistry, Tokyo University of Agriculture Hazardous Chemicals Division, Institute for Agro-Environmental Sciences, NARO
  • Matsushima Yoshitaka
    Department of Agricultural Chemistry, Tokyo University of Agriculture
  • Iwasaki Akio
    Juntendo Medical Technology Innovation Center, Juntendo University
  • Tanaka Naoto
    Department of Molecular Microbiology, Tokyo University of Agriculture
  • Kanesaki Yu
    Genome Research Center, NODAI Research Institute, Tokyo University of Agriculture
  • Martin-Laurent Fabrice
    UMR AgroEcologie, INRA, AgroSup Dijon, University of Bourgogne Franche-Comté
  • Igimi Shizunobu
    Department of Agricultural Chemistry, Tokyo University of Agriculture

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Other Title
  • グラム陽性細菌<i>Nocardioides</i> sp. PD653株における新規PCP脱塩素酵素遺伝子群の同定
  • Identification of the novel hcbB operon catalyzing the dechlorination of pentachlorophenol in the Gram-positive bacterium Nocardioides sp. strain PD653

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Abstract

<p>While pcp genes are well known in Gram-negative bacteria to code for the enzymes responsible for pentachlorophenol (C6HCl5O; PCP) degradation, little is known about PCP-degrading genes in Gram-positive bacteria. Here we describe a novel gene operon possibly responsible for catalyzing the degradation of PCP in the Gram-positive bacterium Nocardioides sp. strain PD653, which is capable of mineralizing hexachlorobenzene (C6Cl6; HCB) via PCP. Transcriptome analysis based on RNA-Seq revealed overexpressed genes in strain PD653 following exposure to HCB. Based on in silico annotation, three open reading frames (ORFs) were selected as biodegrading enzyme candidates. Recombinant E. coli cells expressing candidate genes degraded approximately 9.4 µmol L−1 PCP in 2 hr. Therefore, we designated these genes as hcbB1, hcbB2, and hcbB3. Interestingly, PCP-degrading activity was recorded when hcbB3 was coexpressed with hcbB1 or hcbB2, and the function of HcbB3 was expected to be similar to chlorophenol 4-monooxygenase (TftD).</p>

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