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Arrangement and regulation of the genes for meta-pathway enzymes required for degradation of phenol in Comamonas testosteroni TA441

Laboratory of Microbiology, The Institute of Physical and Chemical Research (RIKEN), Hirosawa 2-1, Wako, Saitama 351-0198, Japan¹

Author for correspondence: Toshiaki Kudo. Tel: +81 48 467 9544. Fax: +81 48 462 4672. e-mail: tkudo{at}postman.riken.go.jp

Comamonas testosteroni TA441 degrades phenol by a meta-cleavage pathway after the occurrence of a spontaneous mutation that derepresses the aphKLMNOPQB operon encoding phenol hydroxylase and catechol 2,3-dioxygenase, the enzymes for the initial two steps of the degradation pathway. A gene cluster, aphCEFGHJI, encoding the meta-pathway enzymes for degradation of 2-hydroxymuconic semialdehyde (HMS) to TCA cycle intermediates was found downstream of the aphK operon. The upstream operon and the downstream gene cluster were found to be separated by two open reading frames of unknown function and an oppositely oriented aphT gene, which is similar to regulatory genes for ortho-cleavage of catechol or chlorinated catechols. A promoter assay using an aphC::lacZ transcriptional fusion plasmid revealed that the aphC promoter activity is induced by both phenol and HMS. The phenol-dependent induction was mediated by AphR and the HMS-dependent induction was mediated by AphT. The aphC promoter in strain TA441 was not silenced, unlike the cases of the aphK and aphR promoters, and was highly induced by HMS.

Keywords: phenol, meta-pathway, biodegradation, Comamonas testosteroni

Abbreviations: 3HPP, 3-(3-hydroxyphenyl)propionate; 4OD, 4-oxalocrotonate decarboxylase; 4OI, 4-oxalocrotonate isomerase; ADA, acetaldehyde dehydrogenase (acylating); C23O, catechol 2,3-dioxygenase; CFE, cell-free extract; HMS, 2-hydroxymuconic semialdehyde; HMSD, HMS dehydrogenase; HMSH, HMS hydrolase; HOA, 4-hydroxy-2-oxovalerate aldolase; OEH, 2-oxopent-4-dienoate hydratase; pHB, p-hydroxybenzoate; PH, phenol hydroxylase

The DDBJ/EMBL/GenBank accession number for the sequence reported in this paper is AB029044.

^a Present address: Department of Biotechnology, University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657, Japan.

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