YaeT-independent multimerization and outer membrane association of secretin PulD
Previous studies demonstrated that targeting of the dodecameric secretin PulD to the Escherichia coli outer membrane is strictly dependent on the chaperone-like pilotin PulS. Here, we report that PulD multimerization and membrane association in strains producing PulS were unaffected when the levels...
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| Veröffentlicht in: | Molecular microbiology 2007-06, Vol.64 (5), p.1350-1357 |
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| creator | Collin, Séverine Guilvout, Ingrid Chami, Mohamed Pugsley, Anthony P |
| description | Previous studies demonstrated that targeting of the dodecameric secretin PulD to the Escherichia coli outer membrane is strictly dependent on the chaperone-like pilotin PulS. Here, we report that PulD multimerization and membrane association in strains producing PulS were unaffected when the levels of the essential outer membrane assembly factor YaeT(Omp85) were reduced by controlled expression of a paraBAD-yaeT transcriptional fusion. This behaviour contrasted markedly to that of the trimeric porin LamB, which remained monomeric under these conditions. Furthermore, resistance to extraction by the detergent Sarkosyl and by urea, and susceptibility to trypsin digestion all suggested that PulD localized to the outer membrane in YaeT-depleted cells. We conclude that, unlike classical β-barrel outer membrane proteins such as LamB, multimerization of PulD is largely YaeT-independent. |
| doi_str_mv | 10.1111/j.1365-2958.2007.05743.x |
| format | Article |
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Here, we report that PulD multimerization and membrane association in strains producing PulS were unaffected when the levels of the essential outer membrane assembly factor YaeT(Omp85) were reduced by controlled expression of a paraBAD-yaeT transcriptional fusion. This behaviour contrasted markedly to that of the trimeric porin LamB, which remained monomeric under these conditions. Furthermore, resistance to extraction by the detergent Sarkosyl and by urea, and susceptibility to trypsin digestion all suggested that PulD localized to the outer membrane in YaeT-depleted cells. We conclude that, unlike classical β-barrel outer membrane proteins such as LamB, multimerization of PulD is largely YaeT-independent.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2007.05743.x</identifier><identifier>PMID: 17542925</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Artificial Gene Fusion ; Bacterial Outer Membrane Proteins - chemistry ; Bacterial Outer Membrane Proteins - genetics ; Bacterial Outer Membrane Proteins - metabolism ; Bacterial Outer Membrane Proteins - ultrastructure ; Bacterial proteins ; Bacteriology ; Biological and medical sciences ; Cell Membrane - drug effects ; Cell Membrane - metabolism ; Cell Membrane - ultrastructure ; Detergents - pharmacology ; E coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Escherichia coli Proteins - ultrastructure ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Membranes ; Microbiology ; Porins - metabolism ; Protein Binding ; Protein Structure, Tertiary ; Receptors, Virus - metabolism ; Sarcosine - analogs & derivatives ; Sarcosine - pharmacology ; Trypsin - pharmacology ; Urea - pharmacology</subject><ispartof>Molecular microbiology, 2007-06, Vol.64 (5), p.1350-1357</ispartof><rights>2007 INIST-CNRS</rights><rights>Copyright Blackwell Publishing Jun 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4173-92884558cf41a2ad3b9105b6fb69ebe3fdf4d4c412c10aeee0fb3d76eaf59f6f3</citedby><cites>FETCH-LOGICAL-c4173-92884558cf41a2ad3b9105b6fb69ebe3fdf4d4c412c10aeee0fb3d76eaf59f6f3</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.1365-2958.2007.05743.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.2007.05743.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,777,781,1412,1428,27905,27906,45555,45556,46390,46814</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18777292$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17542925$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Collin, Séverine</creatorcontrib><creatorcontrib>Guilvout, Ingrid</creatorcontrib><creatorcontrib>Chami, Mohamed</creatorcontrib><creatorcontrib>Pugsley, Anthony P</creatorcontrib><title>YaeT-independent multimerization and outer membrane association of secretin PulD</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Previous studies demonstrated that targeting of the dodecameric secretin PulD to the Escherichia coli outer membrane is strictly dependent on the chaperone-like pilotin PulS. Here, we report that PulD multimerization and membrane association in strains producing PulS were unaffected when the levels of the essential outer membrane assembly factor YaeT(Omp85) were reduced by controlled expression of a paraBAD-yaeT transcriptional fusion. This behaviour contrasted markedly to that of the trimeric porin LamB, which remained monomeric under these conditions. Furthermore, resistance to extraction by the detergent Sarkosyl and by urea, and susceptibility to trypsin digestion all suggested that PulD localized to the outer membrane in YaeT-depleted cells. We conclude that, unlike classical β-barrel outer membrane proteins such as LamB, multimerization of PulD is largely YaeT-independent.</description><subject>Artificial Gene Fusion</subject><subject>Bacterial Outer Membrane Proteins - chemistry</subject><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Bacterial Outer Membrane Proteins - ultrastructure</subject><subject>Bacterial proteins</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - drug effects</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Membrane - ultrastructure</subject><subject>Detergents - pharmacology</subject><subject>E coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Escherichia coli Proteins - ultrastructure</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Membranes</subject><subject>Microbiology</subject><subject>Porins - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Receptors, Virus - metabolism</subject><subject>Sarcosine - analogs & derivatives</subject><subject>Sarcosine - pharmacology</subject><subject>Trypsin - pharmacology</subject><subject>Urea - pharmacology</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkclKxTAUhoMoeh1eQYvgsjVD0zQLF3IdQVFQQVchbU8klw7XpMXh6U3tRbdmkQTO958TviAUEZyQsI4XCWEZj6nkeUIxFgnmImXJxxqa_RbW0QxLjmOW0-cttO39AmPCcMY20RYRPKWS8hm6f9HwGNu2giWEre2jZqh724CzX7q3XRvptoq6oQcXNdAUTrcQae-70k7lzkQeSge9baP7oT7bRRtG1x72VucOero4f5xfxTd3l9fz05u4TIlgsaR5nnKelyYlmuqKFZJgXmSmyCQUwExl0ioNLC0J1gCATcEqkYE2XJrMsB10OPVduu5tAN-rRTe4NoxURGY89CY4QPkEla7z3oFRS2cb7T4VwWo0qRZqFKZGYWo0qX5Mqo8Q3V_1H4oGqr_gSl0AjlaA9qWuTTBTWv_H5UKIAAbuZOLebQ2f_36Aur29Hm8hfzDlje6UfnVhxtMDHb8SCyElZ-wblmiZMw</recordid><startdate>200706</startdate><enddate>200706</enddate><creator>Collin, Séverine</creator><creator>Guilvout, Ingrid</creator><creator>Chami, Mohamed</creator><creator>Pugsley, Anthony P</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>200706</creationdate><title>YaeT-independent multimerization and outer membrane association of secretin PulD</title><author>Collin, Séverine ; Guilvout, Ingrid ; Chami, Mohamed ; Pugsley, Anthony P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4173-92884558cf41a2ad3b9105b6fb69ebe3fdf4d4c412c10aeee0fb3d76eaf59f6f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Artificial Gene Fusion</topic><topic>Bacterial Outer Membrane Proteins - chemistry</topic><topic>Bacterial Outer Membrane Proteins - genetics</topic><topic>Bacterial Outer Membrane Proteins - metabolism</topic><topic>Bacterial Outer Membrane Proteins - ultrastructure</topic><topic>Bacterial proteins</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Cell Membrane - drug effects</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Membrane - ultrastructure</topic><topic>Detergents - pharmacology</topic><topic>E coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Escherichia coli Proteins - ultrastructure</topic><topic>Fundamental and applied biological sciences. 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| subjects | Artificial Gene Fusion Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - metabolism Bacterial Outer Membrane Proteins - ultrastructure Bacterial proteins Bacteriology Biological and medical sciences Cell Membrane - drug effects Cell Membrane - metabolism Cell Membrane - ultrastructure Detergents - pharmacology E coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Escherichia coli Proteins - ultrastructure Fundamental and applied biological sciences. Psychology Gene expression Membranes Microbiology Porins - metabolism Protein Binding Protein Structure, Tertiary Receptors, Virus - metabolism Sarcosine - analogs & derivatives Sarcosine - pharmacology Trypsin - pharmacology Urea - pharmacology |
| title | YaeT-independent multimerization and outer membrane association of secretin PulD |
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