Structure of a type IV secretion system
The three-dimensional structure of the type IV secretion system encoded by the Escherichia coli R388 conjugative plasmid. Structure of a type IV secretion system This study reports the use of electron microscopy to reconstruct a large, 3-megadalton complex of the bacterial type IV secretion (T4S) sy...
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| Veröffentlicht in: | Nature (London) 2014-04, Vol.508 (7497), p.550-553 |
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| creator | Low, Harry H. Gubellini, Francesca Rivera-Calzada, Angel Braun, Nathalie Connery, Sarah Dujeancourt, Annick Lu, Fang Redzej, Adam Fronzes, Rémi Orlova, Elena V. Waksman, Gabriel |
| description | The three-dimensional structure of the type IV secretion system encoded by the
Escherichia coli
R388 conjugative plasmid.
Structure of a type IV secretion system
This study reports the use of electron microscopy to reconstruct a large, 3-megadalton complex of the bacterial type IV secretion (T4S) system from
Escherichia coli
, made up of eight proteins assembled in an intricate stoichiometric relationship to form a stalk spanning the membrane to unite a core outer-membrane-associated complex with an inner membrane complex. The structure reveals a novel architecture that differs markedly from those known from other bacterial secretion systems. T4S systems are used by many bacterial pathogens to deliver virulence factors and to transfer genetic material and also show potential as a tool for the genetic modification of human cells.
Bacterial type IV secretion systems translocate virulence factors into eukaryotic cells
1
,
2
, distribute genetic material between bacteria and have shown potential as a tool for the genetic modification of human cells
3
. Given the complex choreography of the substrate through the secretion apparatus
4
, the molecular mechanism of the type IV secretion system has proved difficult to dissect in the absence of structural data for the entire machinery. Here we use electron microscopy to reconstruct the type IV secretion system encoded by the
Escherichia coli
R388 conjugative plasmid. We show that eight proteins assemble in an intricate stoichiometric relationship to form an approximately 3 megadalton nanomachine that spans the entire cell envelope. The structure comprises an outer membrane-associated core complex
1
connected by a central stalk to a substantial inner membrane complex that is dominated by a battery of 12 VirB4 ATPase subunits organized as side-by-side hexameric barrels. Our results show a secretion system with markedly different architecture, and consequently mechanism, to other known bacterial secretion systems
1
,
4
,
5
,
6
. |
| doi_str_mv | 10.1038/nature13081 |
| format | Article |
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Escherichia coli
R388 conjugative plasmid.
Structure of a type IV secretion system
This study reports the use of electron microscopy to reconstruct a large, 3-megadalton complex of the bacterial type IV secretion (T4S) system from
Escherichia coli
, made up of eight proteins assembled in an intricate stoichiometric relationship to form a stalk spanning the membrane to unite a core outer-membrane-associated complex with an inner membrane complex. The structure reveals a novel architecture that differs markedly from those known from other bacterial secretion systems. T4S systems are used by many bacterial pathogens to deliver virulence factors and to transfer genetic material and also show potential as a tool for the genetic modification of human cells.
Bacterial type IV secretion systems translocate virulence factors into eukaryotic cells
1
,
2
, distribute genetic material between bacteria and have shown potential as a tool for the genetic modification of human cells
3
. Given the complex choreography of the substrate through the secretion apparatus
4
, the molecular mechanism of the type IV secretion system has proved difficult to dissect in the absence of structural data for the entire machinery. Here we use electron microscopy to reconstruct the type IV secretion system encoded by the
Escherichia coli
R388 conjugative plasmid. We show that eight proteins assemble in an intricate stoichiometric relationship to form an approximately 3 megadalton nanomachine that spans the entire cell envelope. The structure comprises an outer membrane-associated core complex
1
connected by a central stalk to a substantial inner membrane complex that is dominated by a battery of 12 VirB4 ATPase subunits organized as side-by-side hexameric barrels. Our results show a secretion system with markedly different architecture, and consequently mechanism, to other known bacterial secretion systems
1
,
4
,
5
,
6
.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/nature13081</identifier><identifier>PMID: 24670658</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>101/28 ; 631/535 ; Adenosine Triphosphatases ; Adenosine Triphosphatases - chemistry ; Adenosine Triphosphatases - genetics ; Adenosine Triphosphatases - metabolism ; Adenosine Triphosphatases - ultrastructure ; Bacterial proteins ; Bacterial Secretion Systems ; Bacterial Secretion Systems - genetics ; Bacteriology ; Biochemistry, Molecular Biology ; Bioinformatics ; Biological Physics ; Cell Membrane ; Cell Membrane - metabolism ; Cellular Biology ; Chemical Sciences ; Computer Science ; Cristallography ; E coli ; Escherichia coli ; Escherichia coli - chemistry ; Escherichia coli - cytology ; Escherichia coli - genetics ; Escherichia coli - ultrastructure ; Escherichia coli Proteins ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - isolation & purification ; Escherichia coli Proteins - metabolism ; Escherichia coli Proteins - ultrastructure ; Genetic research ; Humanities and Social Sciences ; letter ; Life Sciences ; Microbiological research ; Microscopy ; Microscopy, Electron ; Models, Molecular ; multidisciplinary ; Multiprotein Complexes ; Multiprotein Complexes - chemistry ; Multiprotein Complexes - genetics ; Multiprotein Complexes - metabolism ; Multiprotein Complexes - ultrastructure ; Physics ; Physiological aspects ; Science ; Structural Biology ; Symmetry ; Translocation (Genetics) ; Virulence (Microbiology)</subject><ispartof>Nature (London), 2014-04, Vol.508 (7497), p.550-553</ispartof><rights>Springer Nature Limited 2014</rights><rights>COPYRIGHT 2014 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Apr 24, 2014</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c686t-7e349efbb14f83fd78c4af933d64d4c1e6d0cc4a41d871f06e9f017691143cef3</citedby><cites>FETCH-LOGICAL-c686t-7e349efbb14f83fd78c4af933d64d4c1e6d0cc4a41d871f06e9f017691143cef3</cites><orcidid>0000-0003-3031-9824 ; 0000-0003-0708-2726</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nature13081$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nature13081$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24670658$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://pasteur.hal.science/pasteur-03264462$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Low, Harry H.</creatorcontrib><creatorcontrib>Gubellini, Francesca</creatorcontrib><creatorcontrib>Rivera-Calzada, Angel</creatorcontrib><creatorcontrib>Braun, Nathalie</creatorcontrib><creatorcontrib>Connery, Sarah</creatorcontrib><creatorcontrib>Dujeancourt, Annick</creatorcontrib><creatorcontrib>Lu, Fang</creatorcontrib><creatorcontrib>Redzej, Adam</creatorcontrib><creatorcontrib>Fronzes, Rémi</creatorcontrib><creatorcontrib>Orlova, Elena V.</creatorcontrib><creatorcontrib>Waksman, Gabriel</creatorcontrib><title>Structure of a type IV secretion system</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>The three-dimensional structure of the type IV secretion system encoded by the
Escherichia coli
R388 conjugative plasmid.
Structure of a type IV secretion system
This study reports the use of electron microscopy to reconstruct a large, 3-megadalton complex of the bacterial type IV secretion (T4S) system from
Escherichia coli
, made up of eight proteins assembled in an intricate stoichiometric relationship to form a stalk spanning the membrane to unite a core outer-membrane-associated complex with an inner membrane complex. The structure reveals a novel architecture that differs markedly from those known from other bacterial secretion systems. T4S systems are used by many bacterial pathogens to deliver virulence factors and to transfer genetic material and also show potential as a tool for the genetic modification of human cells.
Bacterial type IV secretion systems translocate virulence factors into eukaryotic cells
1
,
2
, distribute genetic material between bacteria and have shown potential as a tool for the genetic modification of human cells
3
. Given the complex choreography of the substrate through the secretion apparatus
4
, the molecular mechanism of the type IV secretion system has proved difficult to dissect in the absence of structural data for the entire machinery. Here we use electron microscopy to reconstruct the type IV secretion system encoded by the
Escherichia coli
R388 conjugative plasmid. We show that eight proteins assemble in an intricate stoichiometric relationship to form an approximately 3 megadalton nanomachine that spans the entire cell envelope. The structure comprises an outer membrane-associated core complex
1
connected by a central stalk to a substantial inner membrane complex that is dominated by a battery of 12 VirB4 ATPase subunits organized as side-by-side hexameric barrels. Our results show a secretion system with markedly different architecture, and consequently mechanism, to other known bacterial secretion systems
1
,
4
,
5
,
6
.</description><subject>101/28</subject><subject>631/535</subject><subject>Adenosine Triphosphatases</subject><subject>Adenosine Triphosphatases - chemistry</subject><subject>Adenosine Triphosphatases - genetics</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Adenosine Triphosphatases - ultrastructure</subject><subject>Bacterial proteins</subject><subject>Bacterial Secretion Systems</subject><subject>Bacterial Secretion Systems - genetics</subject><subject>Bacteriology</subject><subject>Biochemistry, Molecular Biology</subject><subject>Bioinformatics</subject><subject>Biological Physics</subject><subject>Cell Membrane</subject><subject>Cell Membrane - metabolism</subject><subject>Cellular Biology</subject><subject>Chemical Sciences</subject><subject>Computer Science</subject><subject>Cristallography</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Escherichia coli - chemistry</subject><subject>Escherichia coli - 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ultrastructure</subject><subject>Physics</subject><subject>Physiological aspects</subject><subject>Science</subject><subject>Structural Biology</subject><subject>Symmetry</subject><subject>Translocation (Genetics)</subject><subject>Virulence 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Francesca</au><au>Rivera-Calzada, Angel</au><au>Braun, Nathalie</au><au>Connery, Sarah</au><au>Dujeancourt, Annick</au><au>Lu, Fang</au><au>Redzej, Adam</au><au>Fronzes, Rémi</au><au>Orlova, Elena V.</au><au>Waksman, Gabriel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of a type IV secretion system</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>2014-04-24</date><risdate>2014</risdate><volume>508</volume><issue>7497</issue><spage>550</spage><epage>553</epage><pages>550-553</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>The three-dimensional structure of the type IV secretion system encoded by the
Escherichia coli
R388 conjugative plasmid.
Structure of a type IV secretion system
This study reports the use of electron microscopy to reconstruct a large, 3-megadalton complex of the bacterial type IV secretion (T4S) system from
Escherichia coli
, made up of eight proteins assembled in an intricate stoichiometric relationship to form a stalk spanning the membrane to unite a core outer-membrane-associated complex with an inner membrane complex. The structure reveals a novel architecture that differs markedly from those known from other bacterial secretion systems. T4S systems are used by many bacterial pathogens to deliver virulence factors and to transfer genetic material and also show potential as a tool for the genetic modification of human cells.
Bacterial type IV secretion systems translocate virulence factors into eukaryotic cells
1
,
2
, distribute genetic material between bacteria and have shown potential as a tool for the genetic modification of human cells
3
. Given the complex choreography of the substrate through the secretion apparatus
4
, the molecular mechanism of the type IV secretion system has proved difficult to dissect in the absence of structural data for the entire machinery. Here we use electron microscopy to reconstruct the type IV secretion system encoded by the
Escherichia coli
R388 conjugative plasmid. We show that eight proteins assemble in an intricate stoichiometric relationship to form an approximately 3 megadalton nanomachine that spans the entire cell envelope. The structure comprises an outer membrane-associated core complex
1
connected by a central stalk to a substantial inner membrane complex that is dominated by a battery of 12 VirB4 ATPase subunits organized as side-by-side hexameric barrels. Our results show a secretion system with markedly different architecture, and consequently mechanism, to other known bacterial secretion systems
1
,
4
,
5
,
6
.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>24670658</pmid><doi>10.1038/nature13081</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0003-3031-9824</orcidid><orcidid>https://orcid.org/0000-0003-0708-2726</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 2014-04, Vol.508 (7497), p.550-553 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3998870 |
| source | MEDLINE; Nature; SpringerLink (Online service) |
| subjects | 101/28 631/535 Adenosine Triphosphatases Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Adenosine Triphosphatases - ultrastructure Bacterial proteins Bacterial Secretion Systems Bacterial Secretion Systems - genetics Bacteriology Biochemistry, Molecular Biology Bioinformatics Biological Physics Cell Membrane Cell Membrane - metabolism Cellular Biology Chemical Sciences Computer Science Cristallography E coli Escherichia coli Escherichia coli - chemistry Escherichia coli - cytology Escherichia coli - genetics Escherichia coli - ultrastructure Escherichia coli Proteins Escherichia coli Proteins - chemistry Escherichia coli Proteins - isolation & purification Escherichia coli Proteins - metabolism Escherichia coli Proteins - ultrastructure Genetic research Humanities and Social Sciences letter Life Sciences Microbiological research Microscopy Microscopy, Electron Models, Molecular multidisciplinary Multiprotein Complexes Multiprotein Complexes - chemistry Multiprotein Complexes - genetics Multiprotein Complexes - metabolism Multiprotein Complexes - ultrastructure Physics Physiological aspects Science Structural Biology Symmetry Translocation (Genetics) Virulence (Microbiology) |
| title | Structure of a type IV secretion system |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T20%3A20%3A10IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structure%20of%20a%20type%20IV%20secretion%20system&rft.jtitle=Nature%20(London)&rft.au=Low,%20Harry%20H.&rft.date=2014-04-24&rft.volume=508&rft.issue=7497&rft.spage=550&rft.epage=553&rft.pages=550-553&rft.issn=0028-0836&rft.eissn=1476-4687&rft.coden=NATUAS&rft_id=info:doi/10.1038/nature13081&rft_dat=%3Cgale_pubme%3EA366863840%3C/gale_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1523911018&rft_id=info:pmid/24670658&rft_galeid=A366863840&rfr_iscdi=true |