A Protein Export Pathway Involving Escherichia coli Porins
Escherichia coli export the protein YebF into the extracellular medium by a two-step process. However, as no general outer membrane protein secretion system common to all E. coli strains has been reported, the mechanism of export has remained unclear. Herein, we identify the outer membrane proteins...
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| Veröffentlicht in: | Structure (London) 2012-07, Vol.20 (7), p.1154-1166 |
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| creator | Prehna, Gerd Zhang, Guijin Gong, Xiandi Duszyk, Marek Okon, Mark McIntosh, Lawrence P. Weiner, Joel H. Strynadka, Natalie C.J. |
| description | Escherichia coli export the protein YebF into the extracellular medium by a two-step process. However, as no general outer membrane protein secretion system common to all E. coli strains has been reported, the mechanism of export has remained unclear. Herein, we identify the outer membrane proteins OmpF, OmpC, and OmpX as central to the YebF export mechanism using both genetic and planar lipid bilayer experiments. The nuclear magnetic resonance structural ensemble of YebF reveals a cystatin-like fold consisting of a structured core and an extended dynamic surface in a state of conformational exchange. This surface, conserved throughout YebF orthologs of Enterobacteriaceae, may facilitate the porin-mediated transport of YebF as amino acid substitutions of dynamic residues reduced secretion to the extracellular medium. Our results demonstrate that OmpF and OmpC not only operate to import ions and protein toxins but may also contribute to the export of the YebF protein family.
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► The porin OmpF is a required element for the secretion of YebF ► YebF interacts with OmpF and OmpC channels at their periplasmic face ► YebF exhibits a dynamic surface that is involved in the secretion process ► Proposed model of YebF secretion mediated by OmpF |
| doi_str_mv | 10.1016/j.str.2012.04.014 |
| format | Article |
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[Display omitted]
► The porin OmpF is a required element for the secretion of YebF ► YebF interacts with OmpF and OmpC channels at their periplasmic face ► YebF exhibits a dynamic surface that is involved in the secretion process ► Proposed model of YebF secretion mediated by OmpF</description><identifier>ISSN: 0969-2126</identifier><identifier>EISSN: 1878-4186</identifier><identifier>DOI: 10.1016/j.str.2012.04.014</identifier><identifier>PMID: 22658749</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Bacterial Outer Membrane Proteins - chemistry ; Bacterial Outer Membrane Proteins - genetics ; Bacterial Outer Membrane Proteins - metabolism ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Hydrolases - chemistry ; Hydrolases - genetics ; Hydrolases - metabolism ; Lipid Bilayers - chemistry ; Lipid Bilayers - metabolism ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Plasmids ; Porins - chemistry ; Porins - genetics ; Porins - metabolism ; Protein Structure, Secondary ; Protein Transport ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Sequence Alignment ; Static Electricity ; Transformation, Bacterial</subject><ispartof>Structure (London), 2012-07, Vol.20 (7), p.1154-1166</ispartof><rights>2012 Elsevier Ltd</rights><rights>Copyright © 2012 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c462t-ae54728d1a67d9e096ac46dbc118cf4496b66dfbe0787487da1a81c175ea057e3</citedby><cites>FETCH-LOGICAL-c462t-ae54728d1a67d9e096ac46dbc118cf4496b66dfbe0787487da1a81c175ea057e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.str.2012.04.014$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22658749$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Prehna, Gerd</creatorcontrib><creatorcontrib>Zhang, Guijin</creatorcontrib><creatorcontrib>Gong, Xiandi</creatorcontrib><creatorcontrib>Duszyk, Marek</creatorcontrib><creatorcontrib>Okon, Mark</creatorcontrib><creatorcontrib>McIntosh, Lawrence P.</creatorcontrib><creatorcontrib>Weiner, Joel H.</creatorcontrib><creatorcontrib>Strynadka, Natalie C.J.</creatorcontrib><title>A Protein Export Pathway Involving Escherichia coli Porins</title><title>Structure (London)</title><addtitle>Structure</addtitle><description>Escherichia coli export the protein YebF into the extracellular medium by a two-step process. However, as no general outer membrane protein secretion system common to all E. coli strains has been reported, the mechanism of export has remained unclear. Herein, we identify the outer membrane proteins OmpF, OmpC, and OmpX as central to the YebF export mechanism using both genetic and planar lipid bilayer experiments. The nuclear magnetic resonance structural ensemble of YebF reveals a cystatin-like fold consisting of a structured core and an extended dynamic surface in a state of conformational exchange. This surface, conserved throughout YebF orthologs of Enterobacteriaceae, may facilitate the porin-mediated transport of YebF as amino acid substitutions of dynamic residues reduced secretion to the extracellular medium. Our results demonstrate that OmpF and OmpC not only operate to import ions and protein toxins but may also contribute to the export of the YebF protein family.
[Display omitted]
► The porin OmpF is a required element for the secretion of YebF ► YebF interacts with OmpF and OmpC channels at their periplasmic face ► YebF exhibits a dynamic surface that is involved in the secretion process ► Proposed model of YebF secretion mediated by OmpF</description><subject>Amino Acid Sequence</subject><subject>Bacterial Outer Membrane Proteins - chemistry</subject><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Bacterial Outer Membrane Proteins - metabolism</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>Hydrolases - chemistry</subject><subject>Hydrolases - genetics</subject><subject>Hydrolases - metabolism</subject><subject>Lipid Bilayers - chemistry</subject><subject>Lipid Bilayers - metabolism</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Plasmids</subject><subject>Porins - chemistry</subject><subject>Porins - genetics</subject><subject>Porins - metabolism</subject><subject>Protein Structure, Secondary</subject><subject>Protein Transport</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Static Electricity</subject><subject>Transformation, Bacterial</subject><issn>0969-2126</issn><issn>1878-4186</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFOAjEQhhujEUQfwIvZo5dd29Jtu3oyBJWERA56brrtICXLFtsF5e0tAT16msN8_5-ZD6FrgguCCb9bFrELBcWEFpgVmLAT1CdSyJwRyU9RH1e8yimhvIcuYlxijGmJ8TnqUcpLKVjVR_eP2Sz4Dlybjb_XPnTZTHeLL73LJu3WN1vXfmTjaBYQnFk4nRnfuGzmg2vjJTqb6ybC1XEO0PvT-G30kk9fnyejx2luGKddrqFkgkpLNBe2gnSTTgtbG0KkmTNW8ZpzO68Bi3SSFFYTLYkhogSNSwHDAbo99K6D_9xA7NTKRQNNo1vwm6gIpmzIqiHmCSUH1AQfY4C5Wge30mGXILVXppYqKVN7ZQozlZSlzM2xflOvwP4lfh0l4OEAQHpy6yCoaBy0BqwLYDplvfun_gfjCXt5</recordid><startdate>20120703</startdate><enddate>20120703</enddate><creator>Prehna, Gerd</creator><creator>Zhang, Guijin</creator><creator>Gong, Xiandi</creator><creator>Duszyk, Marek</creator><creator>Okon, Mark</creator><creator>McIntosh, Lawrence P.</creator><creator>Weiner, Joel H.</creator><creator>Strynadka, Natalie C.J.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>20120703</creationdate><title>A Protein Export Pathway Involving Escherichia coli Porins</title><author>Prehna, Gerd ; Zhang, Guijin ; Gong, Xiandi ; Duszyk, Marek ; Okon, Mark ; McIntosh, Lawrence P. ; Weiner, Joel H. ; Strynadka, Natalie C.J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c462t-ae54728d1a67d9e096ac46dbc118cf4496b66dfbe0787487da1a81c175ea057e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Outer Membrane Proteins - chemistry</topic><topic>Bacterial Outer Membrane Proteins - genetics</topic><topic>Bacterial Outer Membrane Proteins - metabolism</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>Hydrolases - chemistry</topic><topic>Hydrolases - genetics</topic><topic>Hydrolases - metabolism</topic><topic>Lipid Bilayers - chemistry</topic><topic>Lipid Bilayers - metabolism</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Plasmids</topic><topic>Porins - chemistry</topic><topic>Porins - genetics</topic><topic>Porins - metabolism</topic><topic>Protein Structure, Secondary</topic><topic>Protein Transport</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Alignment</topic><topic>Static Electricity</topic><topic>Transformation, Bacterial</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Prehna, Gerd</creatorcontrib><creatorcontrib>Zhang, Guijin</creatorcontrib><creatorcontrib>Gong, Xiandi</creatorcontrib><creatorcontrib>Duszyk, Marek</creatorcontrib><creatorcontrib>Okon, Mark</creatorcontrib><creatorcontrib>McIntosh, Lawrence P.</creatorcontrib><creatorcontrib>Weiner, Joel H.</creatorcontrib><creatorcontrib>Strynadka, Natalie C.J.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Structure (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Prehna, Gerd</au><au>Zhang, Guijin</au><au>Gong, Xiandi</au><au>Duszyk, Marek</au><au>Okon, Mark</au><au>McIntosh, Lawrence P.</au><au>Weiner, Joel H.</au><au>Strynadka, Natalie C.J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Protein Export Pathway Involving Escherichia coli Porins</atitle><jtitle>Structure (London)</jtitle><addtitle>Structure</addtitle><date>2012-07-03</date><risdate>2012</risdate><volume>20</volume><issue>7</issue><spage>1154</spage><epage>1166</epage><pages>1154-1166</pages><issn>0969-2126</issn><eissn>1878-4186</eissn><abstract>Escherichia coli export the protein YebF into the extracellular medium by a two-step process. However, as no general outer membrane protein secretion system common to all E. coli strains has been reported, the mechanism of export has remained unclear. Herein, we identify the outer membrane proteins OmpF, OmpC, and OmpX as central to the YebF export mechanism using both genetic and planar lipid bilayer experiments. The nuclear magnetic resonance structural ensemble of YebF reveals a cystatin-like fold consisting of a structured core and an extended dynamic surface in a state of conformational exchange. This surface, conserved throughout YebF orthologs of Enterobacteriaceae, may facilitate the porin-mediated transport of YebF as amino acid substitutions of dynamic residues reduced secretion to the extracellular medium. Our results demonstrate that OmpF and OmpC not only operate to import ions and protein toxins but may also contribute to the export of the YebF protein family.
[Display omitted]
► The porin OmpF is a required element for the secretion of YebF ► YebF interacts with OmpF and OmpC channels at their periplasmic face ► YebF exhibits a dynamic surface that is involved in the secretion process ► Proposed model of YebF secretion mediated by OmpF</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>22658749</pmid><doi>10.1016/j.str.2012.04.014</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - metabolism Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Hydrolases - chemistry Hydrolases - genetics Hydrolases - metabolism Lipid Bilayers - chemistry Lipid Bilayers - metabolism Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Plasmids Porins - chemistry Porins - genetics Porins - metabolism Protein Structure, Secondary Protein Transport Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Alignment Static Electricity Transformation, Bacterial |
| title | A Protein Export Pathway Involving Escherichia coli Porins |
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