Literature DB >> 22488571

Differential expression of particulate methane monooxygenase genes in the verrucomicrobial methanotroph 'Methylacidiphilum kamchatkense' Kam1.

Helge-André Erikstad1, Sigmund Jensen, T Jeffrey Keen, Nils-Kåre Birkeland.   

Abstract

Methane monooxygenases (MMOs) are oxygen-dependent enzymes that catalyze the oxidation of methane to methanol in the methanotrophic bacteria. The thermoacidophilic verrucomicrobial methanotroph 'Methylacidiphilum kamchatkense' Kam1 contains three complete and phylogenetically distinct copies of the pmoCAB gene cluster apparently organized as operons, each encoding all three subunits of particulate MMO (pMMO), and a truncated pmoCA cluster encoding only two of the subunits. Two of the clusters are present as a tandem array, but the other clusters occur in isolation. Here, the expression of these clusters has been assessed using the four pmoA genes as targets in reverse transcriptase quantitative PCR analysis. One of the pmoA genes, designated pmoA2, is at least 35-fold more strongly transcribed than the other pmoA copies. Growth at suboptimal temperature and pH conditions did not significantly change the transcription pattern, indicating that the pmoCAB2 cluster encodes the functional pMMO under methane-fuelled growth conditions. During growth on methanol, expression of pmoA2 was reduced approximately tenfold as compared to growth on methane, suggesting a role for the alternative carbon substrates in gene regulation.

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Year:  2012        PMID: 22488571     DOI: 10.1007/s00792-012-0439-y

Source DB:  PubMed          Journal:  Extremophiles        ISSN: 1431-0651            Impact factor:   2.395


  27 in total

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2.  Environmental, genomic and taxonomic perspectives on methanotrophic Verrucomicrobia.

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Review 4.  Methanotrophic bacteria.

Authors:  R S Hanson; T E Hanson
Journal:  Microbiol Rev       Date:  1996-06

5.  Expression of individual copies of Methylococcus capsulatus bath particulate methane monooxygenase genes.

Authors:  S Stolyar; M Franke; M E Lidstrom
Journal:  J Bacteriol       Date:  2001-03       Impact factor: 3.490

6.  Enrichment, isolation and some properties of methane-utilizing bacteria.

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Journal:  J Gen Microbiol       Date:  1970-05

7.  Regulation of bacterial methane oxidation: transcription of the soluble methane mono-oxygenase operon of Methylococcus capsulatus (Bath) is repressed by copper ions.

Authors:  A K Nielsen; K Gerdes; H Degn; J C Murrell
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Authors:  Merlin Tchawa Yimga; Peter F Dunfield; Peter Ricke; Jürgen Heyer; Werner Liesack
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Authors:  Chelsea L Murphy; Andriy Sheremet; Peter F Dunfield; John R Spear; Ramunas Stepanauskas; Tanja Woyke; Mostafa S Elshahed; Noha H Youssef
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2.  Metabolic Regulation of "Ca. Methylacidiphilum Fumariolicum" SolV Cells Grown Under Different Nitrogen and Oxygen Limitations.

Authors:  Ahmad F Khadem; Arjan Pol; Adam S Wieczorek; Mike S M Jetten; Huub J M Op den Camp
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3.  Draft Genome Sequence of "Candidatus Methylacidiphilum kamchatkense" Strain Kam1, a Thermoacidophilic Methanotrophic Verrucomicrobium.

Authors:  Helge-André Erikstad; Nils-Kåre Birkeland
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4.  The genomic landscape of the verrucomicrobial methanotroph Methylacidiphilum fumariolicum SolV.

Authors:  Seyed Yahya Anvar; Jeroen Frank; Arjan Pol; Arnoud Schmitz; Ken Kraaijeveld; Johan T den Dunnen; Huub Jm Op den Camp
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Review 5.  Diversity and Habitat Preferences of Cultivated and Uncultivated Aerobic Methanotrophic Bacteria Evaluated Based on pmoA as Molecular Marker.

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6.  Evolutionary History of Copper Membrane Monooxygenases.

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7.  Global Biogeographic Distribution Patterns of Thermoacidophilic Verrucomicrobia Methanotrophs Suggest Allopatric Evolution.

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8.  Complete genome sequence analysis of the thermoacidophilic verrucomicrobial methanotroph "Candidatus Methylacidiphilum kamchatkense" strain Kam1 and comparison with its closest relatives.

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9.  Large freshwater phages with the potential to augment aerobic methane oxidation.

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10.  Genome Sequence of a Thermoacidophilic Methanotroph Belonging to the Verrucomicrobiota Phylum from Geothermal Hot Springs in Yellowstone National Park: A Metagenomic Assembly and Reconstruction.

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