Characterization of thepcbE gene encoding 2-hydroxypenta-2,4-dienoate hydratase inPseudomonas sp. DJ-12 View Full Text


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Article Info

DATE

2000-04

AUTHORS

Jong-Chul Lim, Jeongrai Lee, Jeong Duk Jang, Jai-Yun Lim, Kyung Rak Min, Chi-Kyung Kim, Youngsoo Kim

ABSTRACT

Nucleotide sequence extending 2,3-dihydroxybiphenyl 1,2-dioxygenase gene (pcbC) and 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase gene (pcbD) of Pseudomonas sp. DJ-12 was previously analyzed and the two genes were present in the order of pcbD-pcbC preceded by a promoter from Pseudomonas sp. DJ-12. In this study, a 3.8-kb nucleotide sequence located downstream of the pcbC gene was analyzed to have three open reading frames (ORFs) that are designated as orf1, pcbE and orf2 genes. All of the ORFs were preceded by each ribosome-binding sequence of 5-GGAXA-3 (X=G or A). However, no promoter-like sequence and transcription terminator sequence were found in the analyzed region, downstream of pcbC gene. Therefore, the gene cluster appeared to be present in the order of pcbD-pcbC-orf1-pcbE-orf2 as an operon, which is unique organization characterized so far in biphenyl- and PCB-degrading bacteria. The orf1 gene was composed of 1,224 base pairs which can encode a polypeptide of molecular weight 44,950 containing 405 amino acid residues. A deduced amino acid sequence of the orf1 gene product exhibited 21-33% identity with those of indole dioxygenase and phenol hydroxylase components. The pcbE gene was composed of 783 base pairs encoding 2-hydroxypenta-2,4-dienoate hydratase involved in the 4-chlorobiphenyl catabolism. The orf2 gene was composed of 1,017 base pairs encoding a polypeptide of molecular weight 37,378 containing 338 amino acid residues. A deduced amino acid sequence of the orf2 gene product exhibited 31% identity with that of a nitrilotriacetate monooxygenase component. More... »

PAGES

187-195

References to SciGraph publications

  • 1986-03. Degradation of highly chlorinated PCBs byPseudomonas strain LB400 in JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY
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    http://scigraph.springernature.com/pub.10.1007/bf02975512

    DOI

    http://dx.doi.org/10.1007/bf02975512

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/10836749


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