presence of multiple c-type cytochromes at the surface of the methanotrophic bacterium Methylococcus capsulatus (Bath) is regulated by copper
Identification of surface proteins is essential to understand bacterial communication with its environment. Analysis of the surface-associated proteins of Methylococcus capsulatus (Bath) revealed a highly dynamic structure responding closely to the availability of copper in the medium in the range f...
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| Veröffentlicht in: | Molecular microbiology 2008-10, Vol.70 (1), p.15-26 |
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| creator | Karlsen, O.A Lillehaug, J.R Jensen, H.B |
| description | Identification of surface proteins is essential to understand bacterial communication with its environment. Analysis of the surface-associated proteins of Methylococcus capsulatus (Bath) revealed a highly dynamic structure responding closely to the availability of copper in the medium in the range from ~0 to 10 μM. Several c-type cytochromes, including three novel multihaem proteins, are present at the cellular surface, a feature that is otherwise a peculiarity of dissimilatory metal-reducing bacteria. At low copper concentrations, the cytochrome c₅₅₃o and the cytochrome c₅₅₃o family protein, encoded by the MCA0421 and MCA0423 genes, respectively, are major constituents of the surfaceome and show a fine-tuned copper-dependent regulation of expression. Two novel members of the cytochrome c₅₅₃o family were identified: MCA0338 was abundant between 5 and 10 μM copper, while MCA2259 was detected only in the surface fraction obtained from ~0 μM copper cultures. The presence at the bacterial surface of several c-type cytochromes, generally involved in energy transduction, indicates strongly that redox processes take place at the bacterial surface. Due to the unique role of copper in the biology of M. capsulatus (Bath), it appears that c-type cytochromes have essential functions in copper homeostasis allowing the cells to adapt to varying copper exposure. |
| doi_str_mv | 10.1111/j.1365-2958.2008.06380.x |
| format | Article |
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Analysis of the surface-associated proteins of Methylococcus capsulatus (Bath) revealed a highly dynamic structure responding closely to the availability of copper in the medium in the range from ~0 to 10 μM. Several c-type cytochromes, including three novel multihaem proteins, are present at the cellular surface, a feature that is otherwise a peculiarity of dissimilatory metal-reducing bacteria. At low copper concentrations, the cytochrome c₅₅₃o and the cytochrome c₅₅₃o family protein, encoded by the MCA0421 and MCA0423 genes, respectively, are major constituents of the surfaceome and show a fine-tuned copper-dependent regulation of expression. Two novel members of the cytochrome c₅₅₃o family were identified: MCA0338 was abundant between 5 and 10 μM copper, while MCA2259 was detected only in the surface fraction obtained from ~0 μM copper cultures. The presence at the bacterial surface of several c-type cytochromes, generally involved in energy transduction, indicates strongly that redox processes take place at the bacterial surface. Due to the unique role of copper in the biology of M. capsulatus (Bath), it appears that c-type cytochromes have essential functions in copper homeostasis allowing the cells to adapt to varying copper exposure.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2008.06380.x</identifier><identifier>PMID: 18681943</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Bacteria ; Bacterial Outer Membrane Proteins - genetics ; Bacterial proteins ; Bacteriology ; Biological and medical sciences ; Copper - metabolism ; Cytochrome c Group - genetics ; Electrophoresis, Gel, Two-Dimensional ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Gene Expression Regulation, Bacterial ; Genes ; Heme - chemistry ; Mass Spectrometry ; Methylococcus capsulatus ; Methylococcus capsulatus - genetics ; Methylococcus capsulatus - metabolism ; Microbiology ; Miscellaneous ; Phenotype ; Proteomics ; Sequence Alignment ; Sequence Analysis, Protein</subject><ispartof>Molecular microbiology, 2008-10, Vol.70 (1), p.15-26</ispartof><rights>2008 The Authors. Journal compilation © 2008 Blackwell Publishing Ltd</rights><rights>2008 INIST-CNRS</rights><rights>Copyright Blackwell Publishing Ltd. 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Analysis of the surface-associated proteins of Methylococcus capsulatus (Bath) revealed a highly dynamic structure responding closely to the availability of copper in the medium in the range from ~0 to 10 μM. Several c-type cytochromes, including three novel multihaem proteins, are present at the cellular surface, a feature that is otherwise a peculiarity of dissimilatory metal-reducing bacteria. At low copper concentrations, the cytochrome c₅₅₃o and the cytochrome c₅₅₃o family protein, encoded by the MCA0421 and MCA0423 genes, respectively, are major constituents of the surfaceome and show a fine-tuned copper-dependent regulation of expression. Two novel members of the cytochrome c₅₅₃o family were identified: MCA0338 was abundant between 5 and 10 μM copper, while MCA2259 was detected only in the surface fraction obtained from ~0 μM copper cultures. The presence at the bacterial surface of several c-type cytochromes, generally involved in energy transduction, indicates strongly that redox processes take place at the bacterial surface. Due to the unique role of copper in the biology of M. capsulatus (Bath), it appears that c-type cytochromes have essential functions in copper homeostasis allowing the cells to adapt to varying copper exposure.</description><subject>Bacteria</subject><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Bacterial proteins</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Copper - metabolism</subject><subject>Cytochrome c Group - genetics</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Genes</subject><subject>Heme - chemistry</subject><subject>Mass Spectrometry</subject><subject>Methylococcus capsulatus</subject><subject>Methylococcus capsulatus - genetics</subject><subject>Methylococcus capsulatus - metabolism</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Phenotype</subject><subject>Proteomics</subject><subject>Sequence Alignment</subject><subject>Sequence Analysis, Protein</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkk1v1DAQhiMEokvhL4CFBIJDgr_iOAcOUPFRqSsOUImb5cxOulkl62A7ovkR_GccsioSJ3yZsed5x2O9zjLCaMHSenMomFBlzutSF5xSXVAlNC1u72Wbu8L9bEPrkuZC8-9n2aMQDpQykcCH2RnTSrNaik32a_QY8AhIXEuGqY_d2COBPM5jCnN0sPduwEBsJHGPJEy-tSu9bAeMe3t00btx3wFpLET03TSQbSrMvQMHMAUCdgxTb2NKX723cf-adIF4vFnOcEeamYAbR_SPswet7QM-OcXz7Prjh28Xn_OrL58uL95d5VAqmZ4kpFY7ZhsEaJpdhSAYVMhsZWulgWmNXIGsWltWrC5VYiVnDXAErriS4jx7ufYdvfsxYYhm6AJg39sjuikYzmgpRVkn8Pk_4MFN_phmM6xWpWRcigTpFQLvQvDYmtF3g_WzYdQsfpmDWWwxiy1m8cv88cvcJunTU_-pGXD3V3gyKAEvToANYPvW2yN04Y7jVEkmFU_c25X72fU4__cAZru9XLKkf7bqW-uMvfHpjuuvfPkwrBQV17X4DbGQvCs</recordid><startdate>200810</startdate><enddate>200810</enddate><creator>Karlsen, O.A</creator><creator>Lillehaug, J.R</creator><creator>Jensen, H.B</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><general>Blackwell Science</general><scope>FBQ</scope><scope>IQODW</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>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>200810</creationdate><title>presence of multiple c-type cytochromes at the surface of the methanotrophic bacterium Methylococcus capsulatus (Bath) is regulated by copper</title><author>Karlsen, O.A ; Lillehaug, J.R ; Jensen, H.B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5640-33486d1abeccbbd7ec31c7e1a7a968c188e26c47fa5719566d1421bc2ec262643</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Bacteria</topic><topic>Bacterial Outer Membrane Proteins - genetics</topic><topic>Bacterial proteins</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Copper - metabolism</topic><topic>Cytochrome c Group - genetics</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Genes</topic><topic>Heme - chemistry</topic><topic>Mass Spectrometry</topic><topic>Methylococcus capsulatus</topic><topic>Methylococcus capsulatus - genetics</topic><topic>Methylococcus capsulatus - metabolism</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Phenotype</topic><topic>Proteomics</topic><topic>Sequence Alignment</topic><topic>Sequence Analysis, Protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Karlsen, O.A</creatorcontrib><creatorcontrib>Lillehaug, J.R</creatorcontrib><creatorcontrib>Jensen, H.B</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Karlsen, O.A</au><au>Lillehaug, J.R</au><au>Jensen, H.B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>presence of multiple c-type cytochromes at the surface of the methanotrophic bacterium Methylococcus capsulatus (Bath) is regulated by copper</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2008-10</date><risdate>2008</risdate><volume>70</volume><issue>1</issue><spage>15</spage><epage>26</epage><pages>15-26</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Identification of surface proteins is essential to understand bacterial communication with its environment. Analysis of the surface-associated proteins of Methylococcus capsulatus (Bath) revealed a highly dynamic structure responding closely to the availability of copper in the medium in the range from ~0 to 10 μM. Several c-type cytochromes, including three novel multihaem proteins, are present at the cellular surface, a feature that is otherwise a peculiarity of dissimilatory metal-reducing bacteria. At low copper concentrations, the cytochrome c₅₅₃o and the cytochrome c₅₅₃o family protein, encoded by the MCA0421 and MCA0423 genes, respectively, are major constituents of the surfaceome and show a fine-tuned copper-dependent regulation of expression. Two novel members of the cytochrome c₅₅₃o family were identified: MCA0338 was abundant between 5 and 10 μM copper, while MCA2259 was detected only in the surface fraction obtained from ~0 μM copper cultures. The presence at the bacterial surface of several c-type cytochromes, generally involved in energy transduction, indicates strongly that redox processes take place at the bacterial surface. Due to the unique role of copper in the biology of M. capsulatus (Bath), it appears that c-type cytochromes have essential functions in copper homeostasis allowing the cells to adapt to varying copper exposure.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>18681943</pmid><doi>10.1111/j.1365-2958.2008.06380.x</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecular microbiology, 2008-10, Vol.70 (1), p.15-26 |
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| source | MEDLINE; Wiley Open Access; Free Full-Text Journals in Chemistry; EZB Electronic Journals Library; Wiley Blackwell Journals |
| subjects | Bacteria Bacterial Outer Membrane Proteins - genetics Bacterial proteins Bacteriology Biological and medical sciences Copper - metabolism Cytochrome c Group - genetics Electrophoresis, Gel, Two-Dimensional Fundamental and applied biological sciences. Psychology Gene expression Gene Expression Regulation, Bacterial Genes Heme - chemistry Mass Spectrometry Methylococcus capsulatus Methylococcus capsulatus - genetics Methylococcus capsulatus - metabolism Microbiology Miscellaneous Phenotype Proteomics Sequence Alignment Sequence Analysis, Protein |
| title | presence of multiple c-type cytochromes at the surface of the methanotrophic bacterium Methylococcus capsulatus (Bath) is regulated by copper |
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