Identification of the Monooxygenase Gene Clusters Responsible for the Regioselective Oxidation of Phenol to Hydroquinone in Mycobacteria
Autor: | Hisashi Semba, Toshiki Furuya, Satomi Hirose, Kuniki Kino, Hisashi Osanai |
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Rok vydání: | 2011 |
Předmět: |
Sequence analysis
Molecular Sequence Data Mutant Genetics and Molecular Biology Polymerase Chain Reaction Applied Microbiology and Biotechnology Mixed Function Oxygenases Mycobacterium Acetone Bacterial Proteins RNA Ribosomal 16S Gene cluster Mycobacterium goodii Peptide sequence Sequence Deletion Base Sequence Phenol Ecology biology Strain (chemistry) Mycobacterium smegmatis Gene Expression Regulation Bacterial Sequence Analysis DNA Monooxygenase biology.organism_classification Hydroquinones Biochemistry Genes Bacterial Multigene Family Oxidation-Reduction Food Science Biotechnology |
Zdroj: | Applied and Environmental Microbiology. 77:1214-1220 |
ISSN: | 1098-5336 0099-2240 |
DOI: | 10.1128/aem.02316-10 |
Popis: | Mycobacterium goodii strain 12523 is an actinomycete that is able to oxidize phenol regioselectively at the para position to produce hydroquinone. In this study, we investigated the genes responsible for this unique regioselective oxidation. On the basis of the fact that the oxidation activity of M. goodii strain 12523 toward phenol is induced in the presence of acetone, we first identified acetone-induced proteins in this microorganism by two-dimensional electrophoretic analysis. The N-terminal amino acid sequence of one of these acetone-induced proteins shares 100% identity with that of the protein encoded by the open reading frame Msmeg_1971 in Mycobacterium smegmatis strain mc 2 155, whose genome sequence has been determined. Since Msmeg_1971, Msmeg_1972, Msmeg_1973, and Msmeg_1974 constitute a putative binuclear iron monooxygenase gene cluster, we cloned this gene cluster of M. smegmatis strain mc 2 155 and its homologous gene cluster found in M. goodii strain 12523. Sequence analysis of these binuclear iron monooxygenase gene clusters revealed the presence of four genes designated mimABCD , which encode an oxygenase large subunit, a reductase, an oxygenase small subunit, and a coupling protein, respectively. When the mimA gene (Msmeg_1971) of M. smegmatis strain mc 2 155, which was also found to be able to oxidize phenol to hydroquinone, was deleted, this mutant lost the oxidation ability. This ability was restored by introduction of the mimA gene of M. smegmatis strain mc 2 155 or of M. goodii strain 12523 into this mutant. Interestingly, we found that these gene clusters also play essential roles in propane and acetone metabolism in these mycobacteria. |
Databáze: | OpenAIRE |
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