Isolation and characterization of the gene encoding the chloroplast-type ferredoxin component of carbazole 1,9a-dioxygenase from a putative Kordiimonas sp

Rintaro Maeda, Takanori Ishii, Yoshihiko Ito, Azham Bin Zulkharnain, Kenichi Iwata, Toshio Omori

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Carbazole (CAR)-degrading genes (carRAaCBaBb) were isolated from marine CAR-degrading isolate strain OC9 (probably Kordiimonas gwangyangensis) using shotgun cloning experiments and showed 35-65% similarity with previously reported CAR-degrading genes. In addition, a ferredoxin-like gene (carAc) was found downstream of carR, although it was not homologous with any reported ferredoxin components of the CAR 1,9a-dioxygenase (CARDO) system. The carAc-deduced amino acid sequence possessed consensus sequences for chloroplast-type iron-sulfur proteins for binding the [2Fe-2S] cluster. These car genes were arranged in the order of carAcRAaCBaBb, but carRAc and carAaCBaBb genes were the opposite orientation. Escherichia coli JM109 cells harboring pBOC91 (carAa) converted CAR to 2′-aminobiphenyl-2,3-diol at a ratio of 12%, and the transformation ratio of CAR increased from 12 to 100% when carAc was added, indicating that CarAc is the ferredoxin component of the CARDO system in strain OC9. This is the first finding of a chloroplast-type ferredoxin component in a CARDO system. Biotransformation tests with aromatic compounds revealed that the strain OC9 CarAaAc showed activity with polycyclic aromatic hydrocarbons and dioxin compounds and exhibited significant activity for fluorene, unlike previously reported CARDOs.

Original languageEnglish
Pages (from-to)1725-1731
Number of pages7
JournalBiotechnology Letters
Volume32
Issue number11
DOIs
Publication statusPublished - 2010

Fingerprint

Ferredoxins
Gene encoding
Fluorouracil
Genes
Dioxygenases
Iron-Sulfur Proteins
Dioxins
Aromatic compounds
Cloning
Polycyclic Aromatic Hydrocarbons
Polycyclic aromatic hydrocarbons
Escherichia coli
Amino acids
Railroad cars
Sulfur
carbazole
carbazole 1,9a-dioxygenase
Iron
Proteins
Amino Acids

Keywords

  • Car gene cluster
  • Carbazole
  • Carbazole 1,9a-dioxygenase
  • Chloroplast-type ferredoxin

ASJC Scopus subject areas

  • Biotechnology

Cite this

Isolation and characterization of the gene encoding the chloroplast-type ferredoxin component of carbazole 1,9a-dioxygenase from a putative Kordiimonas sp. / Maeda, Rintaro; Ishii, Takanori; Ito, Yoshihiko; Bin Zulkharnain, Azham; Iwata, Kenichi; Omori, Toshio.

In: Biotechnology Letters, Vol. 32, No. 11, 2010, p. 1725-1731.

Research output: Contribution to journalArticle

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abstract = "Carbazole (CAR)-degrading genes (carRAaCBaBb) were isolated from marine CAR-degrading isolate strain OC9 (probably Kordiimonas gwangyangensis) using shotgun cloning experiments and showed 35-65{\%} similarity with previously reported CAR-degrading genes. In addition, a ferredoxin-like gene (carAc) was found downstream of carR, although it was not homologous with any reported ferredoxin components of the CAR 1,9a-dioxygenase (CARDO) system. The carAc-deduced amino acid sequence possessed consensus sequences for chloroplast-type iron-sulfur proteins for binding the [2Fe-2S] cluster. These car genes were arranged in the order of carAcRAaCBaBb, but carRAc and carAaCBaBb genes were the opposite orientation. Escherichia coli JM109 cells harboring pBOC91 (carAa) converted CAR to 2′-aminobiphenyl-2,3-diol at a ratio of 12{\%}, and the transformation ratio of CAR increased from 12 to 100{\%} when carAc was added, indicating that CarAc is the ferredoxin component of the CARDO system in strain OC9. This is the first finding of a chloroplast-type ferredoxin component in a CARDO system. Biotransformation tests with aromatic compounds revealed that the strain OC9 CarAaAc showed activity with polycyclic aromatic hydrocarbons and dioxin compounds and exhibited significant activity for fluorene, unlike previously reported CARDOs.",
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