Function of FlhB, a membrane protein implicated in the bacterial flagellar type III secretion system
The membrane protein FlhB is a highly conserved component of the flagellar secretion system, and it plays an active role in the regulation of protein export. In this study conserved properties of FlhB that are important for its function were investigated. Replacing the flhB gene (or part of the gene...
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| Veröffentlicht in: | PloS one 2013-07, Vol.8 (7), p.e68384 |
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| description | The membrane protein FlhB is a highly conserved component of the flagellar secretion system, and it plays an active role in the regulation of protein export. In this study conserved properties of FlhB that are important for its function were investigated. Replacing the flhB gene (or part of the gene) in Salmonella typhimurium with the flhB gene of the distantly related bacterium Aquifex aeolicus greatly reduces motility. However, motility can be restored to some extent by spontaneous mutations in the part of flhB gene coding for the cytoplasmic domain of Aquifex FlhB. Structural analysis suggests that these mutations destabilize the structure. The secondary structure and stability of the mutated cytoplasmic fragments of FlhB have been studied by circular dichroism spectroscopy. The results suggest that conformational flexibility could be important for FlhB function. An extragenic suppressor mutation in the fliS gene, which decreases the affinity of FliS to FliC, partially restores motility of the FlhB substitution mutants. |
| doi_str_mv | 10.1371/journal.pone.0068384 |
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In this study conserved properties of FlhB that are important for its function were investigated. Replacing the flhB gene (or part of the gene) in Salmonella typhimurium with the flhB gene of the distantly related bacterium Aquifex aeolicus greatly reduces motility. However, motility can be restored to some extent by spontaneous mutations in the part of flhB gene coding for the cytoplasmic domain of Aquifex FlhB. Structural analysis suggests that these mutations destabilize the structure. The secondary structure and stability of the mutated cytoplasmic fragments of FlhB have been studied by circular dichroism spectroscopy. The results suggest that conformational flexibility could be important for FlhB function. An extragenic suppressor mutation in the fliS gene, which decreases the affinity of FliS to FliC, partially restores motility of the FlhB substitution mutants.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0068384</identifier><identifier>PMID: 23874605</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Bacteria ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bioinformatics ; Biology ; Circular dichroism ; Cytoplasm - genetics ; Cytoplasm - metabolism ; Dichroism ; Enzymes ; Flagella ; Flagella - genetics ; Flagella - metabolism ; Flexibility ; Genes ; Genetic engineering ; Genetic suppression ; Kinases ; Membrane proteins ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Molecular Sequence Data ; Motility ; Mutants ; Mutation ; Physics ; Plasmids ; Protein structure ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Transport ; Proteins ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Salmonella ; Salmonella Typhimurium ; Salmonella typhimurium - genetics ; Salmonella typhimurium - metabolism ; Secondary structure ; Secretion ; Sequence Alignment ; Spectroscopy ; Spectrum analysis ; Structural analysis ; Structural stability ; Suppression, Genetic - genetics</subject><ispartof>PloS one, 2013-07, Vol.8 (7), p.e68384</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013. This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-89c89ac33ecb51157dc4395724a6887abf0439cbf298b4f8b620cbadca2edcba3</citedby><cites>FETCH-LOGICAL-c758t-89c89ac33ecb51157dc4395724a6887abf0439cbf298b4f8b620cbadca2edcba3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3708937/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3708937/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23874605$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>van Raaij, Mark J.</contributor><creatorcontrib>Meshcheryakov, Vladimir A</creatorcontrib><creatorcontrib>Barker, Clive S</creatorcontrib><creatorcontrib>Kostyukova, Alla S</creatorcontrib><creatorcontrib>Samatey, Fadel A</creatorcontrib><title>Function of FlhB, a membrane protein implicated in the bacterial flagellar type III secretion system</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The membrane protein FlhB is a highly conserved component of the flagellar secretion system, and it plays an active role in the regulation of protein export. In this study conserved properties of FlhB that are important for its function were investigated. Replacing the flhB gene (or part of the gene) in Salmonella typhimurium with the flhB gene of the distantly related bacterium Aquifex aeolicus greatly reduces motility. However, motility can be restored to some extent by spontaneous mutations in the part of flhB gene coding for the cytoplasmic domain of Aquifex FlhB. Structural analysis suggests that these mutations destabilize the structure. The secondary structure and stability of the mutated cytoplasmic fragments of FlhB have been studied by circular dichroism spectroscopy. The results suggest that conformational flexibility could be important for FlhB function. An extragenic suppressor mutation in the fliS gene, which decreases the affinity of FliS to FliC, partially restores motility of the FlhB substitution mutants.</description><subject>Amino Acid Sequence</subject><subject>Bacteria</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bioinformatics</subject><subject>Biology</subject><subject>Circular dichroism</subject><subject>Cytoplasm - genetics</subject><subject>Cytoplasm - metabolism</subject><subject>Dichroism</subject><subject>Enzymes</subject><subject>Flagella</subject><subject>Flagella - genetics</subject><subject>Flagella - metabolism</subject><subject>Flexibility</subject><subject>Genes</subject><subject>Genetic engineering</subject><subject>Genetic suppression</subject><subject>Kinases</subject><subject>Membrane proteins</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Motility</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Physics</subject><subject>Plasmids</subject><subject>Protein structure</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Salmonella</subject><subject>Salmonella Typhimurium</subject><subject>Salmonella typhimurium - genetics</subject><subject>Salmonella typhimurium - metabolism</subject><subject>Secondary structure</subject><subject>Secretion</subject><subject>Sequence Alignment</subject><subject>Spectroscopy</subject><subject>Spectrum analysis</subject><subject>Structural analysis</subject><subject>Structural stability</subject><subject>Suppression, Genetic - genetics</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNkm-L1DAQxoso3rn6DUQDgiC4a9q02_SNcB6uFg4O_Pc2TNPJbo60qUkq7rc3e9s7tqAgeZHM5DdPJsOTJM9TukpZmb67saPrwawG2-OK0jVnPH-QnKcVy5brjLKHJ-ez5In3N5QWjK_Xj5OzjPEyX9PiPGk3Yy-Dtj2ximzM7sNbAqTDrnHQIxmcDah7orvBaAkBWxKjsEPSgAzoNBiiDGzRGHAk7AckdV0Tj9Lhrajf-4Dd0-SRAuPx2bQvku-bj98uPy-vrj_VlxdXS1kWPCx5JXkFkjGUTZGmRdnKnFVFmeWw5ryERtEYy0ZlFW9yxZv4NdlAKyHDNh7YInl51B2M9WIakBcpq6qCMcrSSNRHorVwIwanO3B7YUGL24R1WwEuaGlQNCkCVqpVLOM5KMZZDkVDeaGavExbGbXeT6-NTRcbwD44MDPR-U2vd2JrfwlWUl6xMgq8mgSc_TmiD_9oeaK2ELvSvbJRTHbaS3GRl5xlRRW5RbL6CxVXi52W0SJKx_ys4M2sIDIBf4ctjN6L-uuX_2evf8zZ1yfsDsGEnbdmPNjBz8H8CEpnvXeo7ieXUnFw-N00xMHhYnJ4LHtxOvX7ojtLsz-Pt_d8</recordid><startdate>20130711</startdate><enddate>20130711</enddate><creator>Meshcheryakov, Vladimir A</creator><creator>Barker, Clive S</creator><creator>Kostyukova, Alla S</creator><creator>Samatey, Fadel A</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20130711</creationdate><title>Function of FlhB, a membrane protein implicated in the bacterial flagellar type III secretion system</title><author>Meshcheryakov, Vladimir A ; Barker, Clive S ; Kostyukova, Alla S ; Samatey, Fadel A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c758t-89c89ac33ecb51157dc4395724a6887abf0439cbf298b4f8b620cbadca2edcba3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Sequence</topic><topic>Bacteria</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bioinformatics</topic><topic>Biology</topic><topic>Circular dichroism</topic><topic>Cytoplasm - genetics</topic><topic>Cytoplasm - metabolism</topic><topic>Dichroism</topic><topic>Enzymes</topic><topic>Flagella</topic><topic>Flagella - genetics</topic><topic>Flagella - metabolism</topic><topic>Flexibility</topic><topic>Genes</topic><topic>Genetic engineering</topic><topic>Genetic suppression</topic><topic>Kinases</topic><topic>Membrane proteins</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Motility</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Physics</topic><topic>Plasmids</topic><topic>Protein structure</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Transport</topic><topic>Proteins</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Salmonella</topic><topic>Salmonella Typhimurium</topic><topic>Salmonella typhimurium - genetics</topic><topic>Salmonella typhimurium - metabolism</topic><topic>Secondary structure</topic><topic>Secretion</topic><topic>Sequence Alignment</topic><topic>Spectroscopy</topic><topic>Spectrum analysis</topic><topic>Structural analysis</topic><topic>Structural stability</topic><topic>Suppression, Genetic - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meshcheryakov, Vladimir A</creatorcontrib><creatorcontrib>Barker, Clive S</creatorcontrib><creatorcontrib>Kostyukova, Alla S</creatorcontrib><creatorcontrib>Samatey, Fadel A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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In this study conserved properties of FlhB that are important for its function were investigated. Replacing the flhB gene (or part of the gene) in Salmonella typhimurium with the flhB gene of the distantly related bacterium Aquifex aeolicus greatly reduces motility. However, motility can be restored to some extent by spontaneous mutations in the part of flhB gene coding for the cytoplasmic domain of Aquifex FlhB. Structural analysis suggests that these mutations destabilize the structure. The secondary structure and stability of the mutated cytoplasmic fragments of FlhB have been studied by circular dichroism spectroscopy. The results suggest that conformational flexibility could be important for FlhB function. An extragenic suppressor mutation in the fliS gene, which decreases the affinity of FliS to FliC, partially restores motility of the FlhB substitution mutants.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23874605</pmid><doi>10.1371/journal.pone.0068384</doi><tpages>e68384</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Bacteria Bacterial Proteins - genetics Bacterial Proteins - metabolism Bioinformatics Biology Circular dichroism Cytoplasm - genetics Cytoplasm - metabolism Dichroism Enzymes Flagella Flagella - genetics Flagella - metabolism Flexibility Genes Genetic engineering Genetic suppression Kinases Membrane proteins Membrane Proteins - genetics Membrane Proteins - metabolism Molecular Sequence Data Motility Mutants Mutation Physics Plasmids Protein structure Protein Structure, Secondary Protein Structure, Tertiary Protein Transport Proteins Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Salmonella Salmonella Typhimurium Salmonella typhimurium - genetics Salmonella typhimurium - metabolism Secondary structure Secretion Sequence Alignment Spectroscopy Spectrum analysis Structural analysis Structural stability Suppression, Genetic - genetics |
| title | Function of FlhB, a membrane protein implicated in the bacterial flagellar type III secretion system |
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