Structural and functional studies on the interaction of GspC and GspD in the type II secretion system
Type II secretion systems (T2SSs) are critical for secretion of many proteins from Gram-negative bacteria. In the T2SS, the outer membrane secretin GspD forms a multimeric pore for translocation of secreted proteins. GspD and the inner membrane protein GspC interact with each other via periplasmic d...
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| Veröffentlicht in: | PLoS pathogens 2011-09, Vol.7 (9), p.e1002228-e1002228 |
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| creator | Korotkov, Konstantin V Johnson, Tanya L Jobling, Michael G Pruneda, Jonathan Pardon, Els Héroux, Annie Turley, Stewart Steyaert, Jan Holmes, Randall K Sandkvist, Maria Hol, Wim G J |
| description | Type II secretion systems (T2SSs) are critical for secretion of many proteins from Gram-negative bacteria. In the T2SS, the outer membrane secretin GspD forms a multimeric pore for translocation of secreted proteins. GspD and the inner membrane protein GspC interact with each other via periplasmic domains. Three different crystal structures of the homology region domain of GspC (GspC(HR)) in complex with either two or three domains of the N-terminal region of GspD from enterotoxigenic Escherichia coli show that GspC(HR) adopts an all-β topology. N-terminal β-strands of GspC and the N0 domain of GspD are major components of the interface between these inner and outer membrane proteins from the T2SS. The biological relevance of the observed GspC-GspD interface is shown by analysis of variant proteins in two-hybrid studies and by the effect of mutations in homologous genes on extracellular secretion and subcellular distribution of GspC in Vibrio cholerae. Substitutions of interface residues of GspD have a dramatic effect on the focal distribution of GspC in V. cholerae. These studies indicate that the GspC(HR)-GspD(N0) interactions observed in the crystal structure are essential for T2SS function. Possible implications of our structures for the stoichiometry of the T2SS and exoprotein secretion are discussed. |
| doi_str_mv | 10.1371/journal.ppat.1002228 |
| format | Article |
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In the T2SS, the outer membrane secretin GspD forms a multimeric pore for translocation of secreted proteins. GspD and the inner membrane protein GspC interact with each other via periplasmic domains. Three different crystal structures of the homology region domain of GspC (GspC(HR)) in complex with either two or three domains of the N-terminal region of GspD from enterotoxigenic Escherichia coli show that GspC(HR) adopts an all-β topology. N-terminal β-strands of GspC and the N0 domain of GspD are major components of the interface between these inner and outer membrane proteins from the T2SS. The biological relevance of the observed GspC-GspD interface is shown by analysis of variant proteins in two-hybrid studies and by the effect of mutations in homologous genes on extracellular secretion and subcellular distribution of GspC in Vibrio cholerae. Substitutions of interface residues of GspD have a dramatic effect on the focal distribution of GspC in V. cholerae. These studies indicate that the GspC(HR)-GspD(N0) interactions observed in the crystal structure are essential for T2SS function. Possible implications of our structures for the stoichiometry of the T2SS and exoprotein secretion are discussed.</description><identifier>ISSN: 1553-7374</identifier><identifier>ISSN: 1553-7366</identifier><identifier>EISSN: 1553-7374</identifier><identifier>DOI: 10.1371/journal.ppat.1002228</identifier><identifier>PMID: 21931548</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacterial Secretion Systems - genetics ; Bacteriology ; BASIC BIOLOGICAL SCIENCES ; Biology ; Cholera ; Cloning, Molecular ; E coli ; Gene Expression Regulation, Bacterial ; Genes ; Genes, Bacterial ; Genetic aspects ; Gram-negative bacteria ; Membrane proteins ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Microbiology ; Molecular Sequence Data ; Mutation ; Parasitology ; Peptide Hydrolases - metabolism ; Physiological aspects ; Protein Structure, Tertiary ; Proteins ; Sequence Analysis, DNA ; Topology ; Translocation ; Two-Hybrid System Techniques ; Vibrio cholerae - genetics ; Vibrio cholerae - metabolism ; Virology</subject><ispartof>PLoS pathogens, 2011-09, Vol.7 (9), p.e1002228-e1002228</ispartof><rights>COPYRIGHT 2011 Public Library of Science</rights><rights>2011 Korotkov et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Korotkov KV, Johnson TL, Jobling MG, Pruneda J, Pardon E, et al. (2011) Structural and Functional Studies on the Interaction of GspC and GspD in the Type II Secretion System. 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In the T2SS, the outer membrane secretin GspD forms a multimeric pore for translocation of secreted proteins. GspD and the inner membrane protein GspC interact with each other via periplasmic domains. Three different crystal structures of the homology region domain of GspC (GspC(HR)) in complex with either two or three domains of the N-terminal region of GspD from enterotoxigenic Escherichia coli show that GspC(HR) adopts an all-β topology. N-terminal β-strands of GspC and the N0 domain of GspD are major components of the interface between these inner and outer membrane proteins from the T2SS. The biological relevance of the observed GspC-GspD interface is shown by analysis of variant proteins in two-hybrid studies and by the effect of mutations in homologous genes on extracellular secretion and subcellular distribution of GspC in Vibrio cholerae. Substitutions of interface residues of GspD have a dramatic effect on the focal distribution of GspC in V. cholerae. These studies indicate that the GspC(HR)-GspD(N0) interactions observed in the crystal structure are essential for T2SS function. Possible implications of our structures for the stoichiometry of the T2SS and exoprotein secretion are discussed.</description><subject>Amino Acid Sequence</subject><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacterial Secretion Systems - genetics</subject><subject>Bacteriology</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Biology</subject><subject>Cholera</subject><subject>Cloning, Molecular</subject><subject>E coli</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Genes</subject><subject>Genes, Bacterial</subject><subject>Genetic aspects</subject><subject>Gram-negative bacteria</subject><subject>Membrane proteins</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Parasitology</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Physiological aspects</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Sequence Analysis, DNA</subject><subject>Topology</subject><subject>Translocation</subject><subject>Two-Hybrid System Techniques</subject><subject>Vibrio cholerae - genetics</subject><subject>Vibrio cholerae - metabolism</subject><subject>Virology</subject><issn>1553-7374</issn><issn>1553-7366</issn><issn>1553-7374</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</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>eNqVk02P0zAQhiMEYpfCP0AQwQFxaLGdxB8XpFWBpdIKJBbOluOMW1dpnLUdRP89bppdbdFekA-2PM_72jP2ZNlLjBa4YPjD1g2-U-2i71VcYIQIIfxRdo6rqpizgpWP763PsmchbBEqcYHp0-yMYFHgquTnGVxHP-g4eNXmqmtyM3Q6WpeM8xCHxkLIXZfHDeS2i-DVGMydyS9DvxwVafEpBUcm7nvIV6s8gPYwkmEfIuyeZ0-MagO8mOZZ9uvL55_Lr_Or75er5cXVXFPO4rwyJQXEmSGcYYagNqAFMpQiXCuOFMWKCFIwUhrdkFpRhFBdAzKAm0I3vJhlr4--feuCnCoUJCZcoJRxSn-WrY5E49RW9t7ulN9Lp6wcN5xfS-Wj1S1IwxvCIIlqXpRCgOKC4VrUtWLG1Jomr4_TaUO9g0ZDF1MZT0xPI53dyLX7LdMjiKoqk8Gbo4EL0cqgbQS90a7rQEeJKWECkQS9m07x7maAEOXOBg1tqzpwQ5BcFIfMKEvk23_IhyswUWuVkrSdcelu-uApLwgVVCDEUKIWD1BpNLCz6YpgbNo_Ebw_ESQmwp-4VkMIcnX94z_Yb6dseWS1dyF4MHf1xUgeGuE2SXloBDk1QpK9uv82d6Lbn1_8BcvwA4k</recordid><startdate>20110901</startdate><enddate>20110901</enddate><creator>Korotkov, Konstantin V</creator><creator>Johnson, Tanya L</creator><creator>Jobling, Michael G</creator><creator>Pruneda, Jonathan</creator><creator>Pardon, Els</creator><creator>Héroux, Annie</creator><creator>Turley, Stewart</creator><creator>Steyaert, Jan</creator><creator>Holmes, Randall K</creator><creator>Sandkvist, Maria</creator><creator>Hol, Wim G J</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>ISN</scope><scope>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope><scope>OIOZB</scope><scope>OTOTI</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20110901</creationdate><title>Structural and functional studies on the interaction of GspC and GspD in the type II secretion system</title><author>Korotkov, Konstantin V ; Johnson, Tanya L ; Jobling, Michael G ; Pruneda, Jonathan ; Pardon, Els ; Héroux, Annie ; Turley, Stewart ; Steyaert, Jan ; Holmes, Randall K ; Sandkvist, Maria ; Hol, Wim G J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c687t-5f46e087f287170ebfec90f6601ba80a61a2923724fcd2ba6000bbe0fe1d3cd83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino Acid Sequence</topic><topic>Bacteria</topic><topic>Bacterial Proteins - 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genetics</topic><topic>Vibrio cholerae - metabolism</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Korotkov, Konstantin V</creatorcontrib><creatorcontrib>Johnson, Tanya L</creatorcontrib><creatorcontrib>Jobling, Michael G</creatorcontrib><creatorcontrib>Pruneda, Jonathan</creatorcontrib><creatorcontrib>Pardon, Els</creatorcontrib><creatorcontrib>Héroux, Annie</creatorcontrib><creatorcontrib>Turley, Stewart</creatorcontrib><creatorcontrib>Steyaert, Jan</creatorcontrib><creatorcontrib>Holmes, Randall K</creatorcontrib><creatorcontrib>Sandkvist, Maria</creatorcontrib><creatorcontrib>Hol, Wim G J</creatorcontrib><creatorcontrib>Brookhaven National Laboratory (BNL), Upton, NY (United States)</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: Canada</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech 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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</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>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV - Hybrid</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PLoS pathogens</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Korotkov, Konstantin V</au><au>Johnson, Tanya L</au><au>Jobling, Michael G</au><au>Pruneda, Jonathan</au><au>Pardon, Els</au><au>Héroux, Annie</au><au>Turley, Stewart</au><au>Steyaert, Jan</au><au>Holmes, Randall K</au><au>Sandkvist, Maria</au><au>Hol, Wim G J</au><au>Kubori, Tomoko</au><aucorp>Brookhaven National Laboratory (BNL), Upton, NY (United States)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural and functional studies on the interaction of GspC and GspD in the type II secretion system</atitle><jtitle>PLoS pathogens</jtitle><addtitle>PLoS Pathog</addtitle><date>2011-09-01</date><risdate>2011</risdate><volume>7</volume><issue>9</issue><spage>e1002228</spage><epage>e1002228</epage><pages>e1002228-e1002228</pages><issn>1553-7374</issn><issn>1553-7366</issn><eissn>1553-7374</eissn><abstract>Type II secretion systems (T2SSs) are critical for secretion of many proteins from Gram-negative bacteria. In the T2SS, the outer membrane secretin GspD forms a multimeric pore for translocation of secreted proteins. GspD and the inner membrane protein GspC interact with each other via periplasmic domains. Three different crystal structures of the homology region domain of GspC (GspC(HR)) in complex with either two or three domains of the N-terminal region of GspD from enterotoxigenic Escherichia coli show that GspC(HR) adopts an all-β topology. N-terminal β-strands of GspC and the N0 domain of GspD are major components of the interface between these inner and outer membrane proteins from the T2SS. The biological relevance of the observed GspC-GspD interface is shown by analysis of variant proteins in two-hybrid studies and by the effect of mutations in homologous genes on extracellular secretion and subcellular distribution of GspC in Vibrio cholerae. Substitutions of interface residues of GspD have a dramatic effect on the focal distribution of GspC in V. cholerae. These studies indicate that the GspC(HR)-GspD(N0) interactions observed in the crystal structure are essential for T2SS function. Possible implications of our structures for the stoichiometry of the T2SS and exoprotein secretion are discussed.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21931548</pmid><doi>10.1371/journal.ppat.1002228</doi><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central Open Access; Public Library of Science (PLoS); PubMed Central |
| subjects | Amino Acid Sequence Bacteria Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacterial Secretion Systems - genetics Bacteriology BASIC BIOLOGICAL SCIENCES Biology Cholera Cloning, Molecular E coli Gene Expression Regulation, Bacterial Genes Genes, Bacterial Genetic aspects Gram-negative bacteria Membrane proteins Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Microbiology Molecular Sequence Data Mutation Parasitology Peptide Hydrolases - metabolism Physiological aspects Protein Structure, Tertiary Proteins Sequence Analysis, DNA Topology Translocation Two-Hybrid System Techniques Vibrio cholerae - genetics Vibrio cholerae - metabolism Virology |
| title | Structural and functional studies on the interaction of GspC and GspD in the type II secretion system |
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