Interactions between C ring proteins and export apparatus components: a possible mechanism for facilitating type III protein export
Summary The flagellar switch proteins of Salmonella, FliG, FliM and FliN, participate in the switching of motor rotation, torque generation and flagellar assembly/export. FliN has been implicated in the flagellar export process. To address this possibility, we constructed 10‐amino‐acid scanning dele...
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| Veröffentlicht in: | Molecular microbiology 2006-05, Vol.60 (4), p.984-998 |
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| creator | González‐Pedrajo, Bertha Minamino, Tohru Kihara, May Namba, Keiichi |
| description | Summary
The flagellar switch proteins of Salmonella, FliG, FliM and FliN, participate in the switching of motor rotation, torque generation and flagellar assembly/export. FliN has been implicated in the flagellar export process. To address this possibility, we constructed 10‐amino‐acid scanning deletions and larger truncations over the C‐terminal domain of FliN. Except for the last deletion variant, all other variants were unable to complement a fliN null strain or to restore the export of flagellar proteins. Most of the deletions showed strong negative dominance effects on wild‐type cells. FliN was found to associate with FliH, a flagellar export component that regulates the ATPase activity of FliI. The binding of FliM to FliN does not interfere with this FliN–FliH interaction. Furthermore, a five‐protein complex consisting of FliG, His‐tagged FliM, FliN, FliH and FliI was purified by nickel‐affinity chromatography. FliJ, a putative general chaperone, is bound to FliM even in the absence of FliH. The importance of the C ring as a possible docking site for export substrates, chaperones and FliI through FliH for their efficient delivery to membrane components of the export apparatus is discussed. |
| doi_str_mv | 10.1111/j.1365-2958.2006.05149.x |
| format | Article |
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The flagellar switch proteins of Salmonella, FliG, FliM and FliN, participate in the switching of motor rotation, torque generation and flagellar assembly/export. FliN has been implicated in the flagellar export process. To address this possibility, we constructed 10‐amino‐acid scanning deletions and larger truncations over the C‐terminal domain of FliN. Except for the last deletion variant, all other variants were unable to complement a fliN null strain or to restore the export of flagellar proteins. Most of the deletions showed strong negative dominance effects on wild‐type cells. FliN was found to associate with FliH, a flagellar export component that regulates the ATPase activity of FliI. The binding of FliM to FliN does not interfere with this FliN–FliH interaction. Furthermore, a five‐protein complex consisting of FliG, His‐tagged FliM, FliN, FliH and FliI was purified by nickel‐affinity chromatography. FliJ, a putative general chaperone, is bound to FliM even in the absence of FliH. The importance of the C ring as a possible docking site for export substrates, chaperones and FliI through FliH for their efficient delivery to membrane components of the export apparatus is discussed.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2006.05149.x</identifier><identifier>PMID: 16677309</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino acids ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biochemistry ; Biological and medical sciences ; Chromatography ; Flagella - metabolism ; Fundamental and applied biological sciences. Psychology ; Genes, Dominant ; Genetic Complementation Test ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Microbiology ; Protein Interaction Mapping ; Protein Transport ; Proteins ; Salmonella ; Salmonella - metabolism ; Sequence Deletion</subject><ispartof>Molecular microbiology, 2006-05, Vol.60 (4), p.984-998</ispartof><rights>2006 INIST-CNRS</rights><rights>Copyright Blackwell Publishing May 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5219-cb53eb6ab7957cc7848036f49c5fdaab04275ec9edfebae95305b4515b574083</citedby><cites>FETCH-LOGICAL-c5219-cb53eb6ab7957cc7848036f49c5fdaab04275ec9edfebae95305b4515b574083</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.1365-2958.2006.05149.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.2006.05149.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17751894$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16677309$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>González‐Pedrajo, Bertha</creatorcontrib><creatorcontrib>Minamino, Tohru</creatorcontrib><creatorcontrib>Kihara, May</creatorcontrib><creatorcontrib>Namba, Keiichi</creatorcontrib><title>Interactions between C ring proteins and export apparatus components: a possible mechanism for facilitating type III protein export</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
The flagellar switch proteins of Salmonella, FliG, FliM and FliN, participate in the switching of motor rotation, torque generation and flagellar assembly/export. FliN has been implicated in the flagellar export process. To address this possibility, we constructed 10‐amino‐acid scanning deletions and larger truncations over the C‐terminal domain of FliN. Except for the last deletion variant, all other variants were unable to complement a fliN null strain or to restore the export of flagellar proteins. Most of the deletions showed strong negative dominance effects on wild‐type cells. FliN was found to associate with FliH, a flagellar export component that regulates the ATPase activity of FliI. The binding of FliM to FliN does not interfere with this FliN–FliH interaction. Furthermore, a five‐protein complex consisting of FliG, His‐tagged FliM, FliN, FliH and FliI was purified by nickel‐affinity chromatography. FliJ, a putative general chaperone, is bound to FliM even in the absence of FliH. The importance of the C ring as a possible docking site for export substrates, chaperones and FliI through FliH for their efficient delivery to membrane components of the export apparatus is discussed.</description><subject>Amino acids</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chromatography</subject><subject>Flagella - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Dominant</subject><subject>Genetic Complementation Test</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Microbiology</subject><subject>Protein Interaction Mapping</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Salmonella</subject><subject>Salmonella - metabolism</subject><subject>Sequence Deletion</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU-P1CAYh4nRuLOrX8EQE721QimlmHgwE1eb7MbLHrwRYN4qk5ZWYLIzZ7-41Klu4kUJCQSe9-HPDyFMSUlze7MvKWt4UUnelhUhTUk4rWV5fIQ2fzYeow2RnBSsrb5coMsY94RQRhr2FF3QphGCEblBPzqfIGib3OQjNpDuATze4uD8VzyHKYHL69rvMBznKSSs51kHnQ4R22mcJw8-xbdY43mK0ZkB8Aj2m_YujrifAu61dYNLOi2-dJoBd133W7w6n6EnvR4iPF_HK3R3_eFu-6m4-fyx276_KSyvqCys4QxMo42QXFgr2rolrOlraXm_09qQuhIcrIRdD0aD5IxwU3PKDRc1adkVen3W5tO_HyAmNbpoYRi0h-kQVSNkNmTnv0AqqtzFAr78C9xPh-DzGxSVDWesqmWG2jNkQ_6iAL2agxt1OClK1JKm2qslNLWEppY01a801TGXvlj9BzPC7qFwjS8Dr1ZAR6uHPmhvXXzghOC0lXXm3p25ezfA6b8voG5vu2XGfgJUgr0D</recordid><startdate>200605</startdate><enddate>200605</enddate><creator>González‐Pedrajo, Bertha</creator><creator>Minamino, Tohru</creator><creator>Kihara, May</creator><creator>Namba, Keiichi</creator><general>Blackwell Publishing Ltd</general><general>Blackwell Science</general><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><scope>7X8</scope></search><sort><creationdate>200605</creationdate><title>Interactions between C ring proteins and export apparatus components: a possible mechanism for facilitating type III protein export</title><author>González‐Pedrajo, Bertha ; Minamino, Tohru ; Kihara, May ; Namba, Keiichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5219-cb53eb6ab7957cc7848036f49c5fdaab04275ec9edfebae95305b4515b574083</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino acids</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chromatography</topic><topic>Flagella - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Dominant</topic><topic>Genetic Complementation Test</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Microbiology</topic><topic>Protein Interaction Mapping</topic><topic>Protein Transport</topic><topic>Proteins</topic><topic>Salmonella</topic><topic>Salmonella - metabolism</topic><topic>Sequence Deletion</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>González‐Pedrajo, Bertha</creatorcontrib><creatorcontrib>Minamino, Tohru</creatorcontrib><creatorcontrib>Kihara, May</creatorcontrib><creatorcontrib>Namba, Keiichi</creatorcontrib><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><collection>MEDLINE - Academic</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>González‐Pedrajo, Bertha</au><au>Minamino, Tohru</au><au>Kihara, May</au><au>Namba, Keiichi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interactions between C ring proteins and export apparatus components: a possible mechanism for facilitating type III protein export</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2006-05</date><risdate>2006</risdate><volume>60</volume><issue>4</issue><spage>984</spage><epage>998</epage><pages>984-998</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
The flagellar switch proteins of Salmonella, FliG, FliM and FliN, participate in the switching of motor rotation, torque generation and flagellar assembly/export. FliN has been implicated in the flagellar export process. To address this possibility, we constructed 10‐amino‐acid scanning deletions and larger truncations over the C‐terminal domain of FliN. Except for the last deletion variant, all other variants were unable to complement a fliN null strain or to restore the export of flagellar proteins. Most of the deletions showed strong negative dominance effects on wild‐type cells. FliN was found to associate with FliH, a flagellar export component that regulates the ATPase activity of FliI. The binding of FliM to FliN does not interfere with this FliN–FliH interaction. Furthermore, a five‐protein complex consisting of FliG, His‐tagged FliM, FliN, FliH and FliI was purified by nickel‐affinity chromatography. FliJ, a putative general chaperone, is bound to FliM even in the absence of FliH. The importance of the C ring as a possible docking site for export substrates, chaperones and FliI through FliH for their efficient delivery to membrane components of the export apparatus is discussed.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>16677309</pmid><doi>10.1111/j.1365-2958.2006.05149.x</doi><tpages>15</tpages></addata></record> |
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| subjects | Amino acids Bacterial Proteins - genetics Bacterial Proteins - metabolism Biochemistry Biological and medical sciences Chromatography Flagella - metabolism Fundamental and applied biological sciences. Psychology Genes, Dominant Genetic Complementation Test Membrane Proteins - genetics Membrane Proteins - metabolism Microbiology Protein Interaction Mapping Protein Transport Proteins Salmonella Salmonella - metabolism Sequence Deletion |
| title | Interactions between C ring proteins and export apparatus components: a possible mechanism for facilitating type III protein export |
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