Evidence for the presence of a CmuA methyltransferase pathway in novel marine methyl halide-oxidizing bacteria

Summary Marine bacteria that oxidized methyl bromide and methyl chloride were enriched and isolated from seawater samples. Six methyl halide‐oxidizing enrichments were established from which 13 isolates that grew on methyl bromide and methyl chloride as sole sources of carbon and energy were isolate...

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Veröffentlicht in:Environmental microbiology 2005-06, Vol.7 (6), p.839-852
Hauptverfasser: Schäfer, Hendrik, McDonald, Ian R., Nightingale, Phil D., Murrell, J. Colin
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container_title Environmental microbiology
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creator Schäfer, Hendrik
McDonald, Ian R.
Nightingale, Phil D.
Murrell, J. Colin
description Summary Marine bacteria that oxidized methyl bromide and methyl chloride were enriched and isolated from seawater samples. Six methyl halide‐oxidizing enrichments were established from which 13 isolates that grew on methyl bromide and methyl chloride as sole sources of carbon and energy were isolated and maintained. All isolates belonged to three different clades in the Roseobacter group of the alpha subdivision of the Proteobacteria and were distinct from Leisingera methylohalidivorans, the only other identified marine bacterium that grows on methyl bromide  as sole source of carbon and energy. Genes  encoding the methyltransferase/corrinoid‐binding protein CmuA, which is responsible for the initial step of methyl chloride oxidation in terrestrial methyl halide‐oxidizing bacteria, were detected in enrichments and some of the novel marine strains. Gene clusters containing cmuA and other genes implicated in the metabolism of methyl halides were cloned from two of the isolates. Expression of CmuA during growth on methyl halides was demonstrated by analysis of polypeptides expressed during growth on methyl halides by SDS‐PAGE and mass spectrometry in two isolates representing two of the three clades. These findings indicate that certain marine methyl halide degrading bacteria from the Roseobacter group contain a methyltransferase pathway for oxidation of methyl bromide that may be similar to that responsible for methyl chloride oxidation in Methylobacterium chloromethanicum. This pathway therefore potentially contributes to cycling of methyl halides in both terrestrial and marine environments.
doi_str_mv 10.1111/j.1462-2920.2005.00757.x
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Gene clusters containing cmuA and other genes implicated in the metabolism of methyl halides were cloned from two of the isolates. Expression of CmuA during growth on methyl halides was demonstrated by analysis of polypeptides expressed during growth on methyl halides by SDS‐PAGE and mass spectrometry in two isolates representing two of the three clades. These findings indicate that certain marine methyl halide degrading bacteria from the Roseobacter group contain a methyltransferase pathway for oxidation of methyl bromide that may be similar to that responsible for methyl chloride oxidation in Methylobacterium chloromethanicum. 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Colin</creatorcontrib><title>Evidence for the presence of a CmuA methyltransferase pathway in novel marine methyl halide-oxidizing bacteria</title><title>Environmental microbiology</title><addtitle>Environ Microbiol</addtitle><description>Summary Marine bacteria that oxidized methyl bromide and methyl chloride were enriched and isolated from seawater samples. Six methyl halide‐oxidizing enrichments were established from which 13 isolates that grew on methyl bromide and methyl chloride as sole sources of carbon and energy were isolated and maintained. All isolates belonged to three different clades in the Roseobacter group of the alpha subdivision of the Proteobacteria and were distinct from Leisingera methylohalidivorans, the only other identified marine bacterium that grows on methyl bromide  as sole source of carbon and energy. Genes  encoding the methyltransferase/corrinoid‐binding protein CmuA, which is responsible for the initial step of methyl chloride oxidation in terrestrial methyl halide‐oxidizing bacteria, were detected in enrichments and some of the novel marine strains. Gene clusters containing cmuA and other genes implicated in the metabolism of methyl halides were cloned from two of the isolates. Expression of CmuA during growth on methyl halides was demonstrated by analysis of polypeptides expressed during growth on methyl halides by SDS‐PAGE and mass spectrometry in two isolates representing two of the three clades. These findings indicate that certain marine methyl halide degrading bacteria from the Roseobacter group contain a methyltransferase pathway for oxidation of methyl bromide that may be similar to that responsible for methyl chloride oxidation in Methylobacterium chloromethanicum. 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Colin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for the presence of a CmuA methyltransferase pathway in novel marine methyl halide-oxidizing bacteria</atitle><jtitle>Environmental microbiology</jtitle><addtitle>Environ Microbiol</addtitle><date>2005-06</date><risdate>2005</risdate><volume>7</volume><issue>6</issue><spage>839</spage><epage>852</epage><pages>839-852</pages><issn>1462-2912</issn><eissn>1462-2920</eissn><abstract>Summary Marine bacteria that oxidized methyl bromide and methyl chloride were enriched and isolated from seawater samples. Six methyl halide‐oxidizing enrichments were established from which 13 isolates that grew on methyl bromide and methyl chloride as sole sources of carbon and energy were isolated and maintained. All isolates belonged to three different clades in the Roseobacter group of the alpha subdivision of the Proteobacteria and were distinct from Leisingera methylohalidivorans, the only other identified marine bacterium that grows on methyl bromide  as sole source of carbon and energy. Genes  encoding the methyltransferase/corrinoid‐binding protein CmuA, which is responsible for the initial step of methyl chloride oxidation in terrestrial methyl halide‐oxidizing bacteria, were detected in enrichments and some of the novel marine strains. Gene clusters containing cmuA and other genes implicated in the metabolism of methyl halides were cloned from two of the isolates. Expression of CmuA during growth on methyl halides was demonstrated by analysis of polypeptides expressed during growth on methyl halides by SDS‐PAGE and mass spectrometry in two isolates representing two of the three clades. 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source MEDLINE; Wiley Online Library Journals Frontfile Complete
subjects Bacterial Proteins - metabolism
Hydrocarbons, Brominated - metabolism
Methyl Chloride - metabolism
Methylobacterium chloromethanicum
Methyltransferases - chemistry
Methyltransferases - genetics
Methyltransferases - metabolism
Proteobacteria
Proteobacteria - classification
Proteobacteria - enzymology
Proteobacteria - genetics
Proteobacteria - growth & development
Roseobacter
Seawater - microbiology
title Evidence for the presence of a CmuA methyltransferase pathway in novel marine methyl halide-oxidizing bacteria
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