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 |
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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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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.</description><identifier>ISSN: 1462-2912</identifier><identifier>EISSN: 1462-2920</identifier><identifier>DOI: 10.1111/j.1462-2920.2005.00757.x</identifier><identifier>PMID: 15892703</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>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</subject><ispartof>Environmental microbiology, 2005-06, Vol.7 (6), p.839-852</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5017-def629a75aa4db1c813b743b868f2d166950e0c9de18b6b49d0df12e00f73d783</citedby><cites>FETCH-LOGICAL-c5017-def629a75aa4db1c813b743b868f2d166950e0c9de18b6b49d0df12e00f73d783</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1462-2920.2005.00757.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1462-2920.2005.00757.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,778,782,1414,27907,27908,45557,45558</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15892703$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schäfer, Hendrik</creatorcontrib><creatorcontrib>McDonald, Ian R.</creatorcontrib><creatorcontrib>Nightingale, Phil D.</creatorcontrib><creatorcontrib>Murrell, J. 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. This pathway therefore potentially contributes to cycling of methyl halides in both terrestrial and marine environments.</description><subject>Bacterial Proteins - metabolism</subject><subject>Hydrocarbons, Brominated - metabolism</subject><subject>Methyl Chloride - metabolism</subject><subject>Methylobacterium chloromethanicum</subject><subject>Methyltransferases - chemistry</subject><subject>Methyltransferases - genetics</subject><subject>Methyltransferases - metabolism</subject><subject>Proteobacteria</subject><subject>Proteobacteria - classification</subject><subject>Proteobacteria - enzymology</subject><subject>Proteobacteria - genetics</subject><subject>Proteobacteria - growth & development</subject><subject>Roseobacter</subject><subject>Seawater - microbiology</subject><issn>1462-2912</issn><issn>1462-2920</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUtP4zAQxy3EannsfgXkE7cEP5LYkbigqjykwu5hEXuznHhMXfIodgotnx6XVuUIvng0_v1nPPNHCFOS0njOZinNCpawkpGUEZKnhIhcpMs9dLh72N_FlB2goxBmhFDBBfmJDmguSyYIP0Td-MUZ6GrAtvd4mAKeewgfid5ijUft4gK3MExXzeB1Fyx4HSKkh-mrXmHX4a5_gQa32rsOtiSe6iZWTfqlM-7NdY-40vUA3ulf6IfVTYDf2_sY3V-O_42uk8mfq5vRxSSp8_jJxIAtWKlFrnVmKlpLyiuR8UoW0jJDi6LMCZC6NEBlVVRZaYixlAEhVnAjJD9Gp5u6c98_LyAMqnWhhqbRHfSLoIrIxA7sS5AKGZvzLIJyA9a-D8GDVXPv4tQrRYlam6Jmar1vtd69WpuiPkxRyyg92fZYVC2YT-HWhQicb4BX18Dq24XV-PYmBlGebOQuDLDcybV_inNykauHuyt1-_86k8Xkr8r4O7fBqts</recordid><startdate>200506</startdate><enddate>200506</enddate><creator>Schäfer, Hendrik</creator><creator>McDonald, Ian R.</creator><creator>Nightingale, Phil D.</creator><creator>Murrell, J. Colin</creator><general>Blackwell Science Ltd</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>200506</creationdate><title>Evidence for the presence of a CmuA methyltransferase pathway in novel marine methyl halide-oxidizing bacteria</title><author>Schäfer, Hendrik ; McDonald, Ian R. ; Nightingale, Phil D. ; Murrell, J. Colin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5017-def629a75aa4db1c813b743b868f2d166950e0c9de18b6b49d0df12e00f73d783</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Bacterial Proteins - metabolism</topic><topic>Hydrocarbons, Brominated - metabolism</topic><topic>Methyl Chloride - metabolism</topic><topic>Methylobacterium chloromethanicum</topic><topic>Methyltransferases - chemistry</topic><topic>Methyltransferases - genetics</topic><topic>Methyltransferases - metabolism</topic><topic>Proteobacteria</topic><topic>Proteobacteria - classification</topic><topic>Proteobacteria - enzymology</topic><topic>Proteobacteria - genetics</topic><topic>Proteobacteria - growth & development</topic><topic>Roseobacter</topic><topic>Seawater - microbiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schäfer, Hendrik</creatorcontrib><creatorcontrib>McDonald, Ian R.</creatorcontrib><creatorcontrib>Nightingale, Phil D.</creatorcontrib><creatorcontrib>Murrell, J. Colin</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Environmental microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schäfer, Hendrik</au><au>McDonald, Ian R.</au><au>Nightingale, Phil D.</au><au>Murrell, J. 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. 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.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>15892703</pmid><doi>10.1111/j.1462-2920.2005.00757.x</doi><tpages>14</tpages></addata></record> |
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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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