Regulation of bacterial methane oxidation: transcription of the soluble methane mono-oxygenase operon of Methylococcus capsulatus (Bath) is repressed by copper ions
Article Abstract:
Copper (Cu) ions suppress the activity of the promoter that controls the transcription of methane mono-oxygenase (MMO) required for the oxidation of methane to methanol in Methylococcus capsulatus (Bath). Cu ions decrease the activity of soluble MMO (sMMO) and the amount of smmo-specific mRNAs. The six open reading frames of the sMMO gene cluster are present as an operon, and the promoter is upstream of the mmoX start codon. The operon produces three transcripts that vary in their 3' ends. The mRNA-1 encodes mmoX; mRNA-2 encodes mmoX, mmoY, mmoB and mmoZ; and mRNA-3 encodes all the mmo cistrons.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
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Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme
Article Abstract:
An M2 strain methylotroph that uses methanesulfonic acid (MSA) as its only source of carbon and energy was investigated. An inducible NADH-specific monooxygenase enzyme played a key role in the first step of the MSA's biodegradative pathway. An analysis of defective M2 strain mutants in the metabolism of C1 compounds showed that methanol was not an intermediate in MSA's degradative pathway. A multicomponent enzyme was found to be involved in MSA degradation by methylotroph strain M2.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
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Homologous expression of soluble methane monooxygenase genes in Methylosinus trichosporium OB3b
Article Abstract:
A study was conducted to analyze a homologous expression system designed fro soluble methane monooxygenase (sMMO) genes from Methylosinus trichosporium OB3b. The complementation of the sMMO-minus genotype was realized by conjugation with broad-host-range plasmids supporting the native promoter and sMMO operon from Ms. trichosporium OB3b. In addition, the plasmids utilized in the study were prepared in Escherichia coli.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1999
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