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A TonB-dependent transporter is required for secretion of protease PopC across the bacterial outer membrane
TonB-dependent transporters (TBDTs) are ubiquitous outer membrane β-barrel proteins that import nutrients and bacteriocins across the outer membrane in a proton motive force-dependent manner, by directly connecting to the ExbB/ExbD/TonB system in the inner membrane. Here, we show that the TBDT Oar i...
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Published in: | Nature communications 2019-03, Vol.10 (1), p.1360-1360, Article 1360 |
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description | TonB-dependent transporters (TBDTs) are ubiquitous outer membrane β-barrel proteins that import nutrients and bacteriocins across the outer membrane in a proton motive force-dependent manner, by directly connecting to the ExbB/ExbD/TonB system in the inner membrane. Here, we show that the TBDT Oar in
Myxococcus xanthus
is required for secretion of a protein, protease PopC, to the extracellular milieu. PopC accumulates in the periplasm before secretion across the outer membrane, and the proton motive force has a role in secretion to the extracellular milieu. Reconstitution experiments in
Escherichia coli
demonstrate that secretion of PopC across the outer membrane not only depends on Oar but also on the ExbB/ExbD/TonB system. Our results indicate that TBDTs and the ExbB/ExbD/TonB system may have roles not only in import processes but also in secretion of proteins.
TonB-dependent transporters (TBDTs) are outer membrane proteins that import nutrients and bacteriocins in bacteria. Here, Gómez-Santos et al. show that a TBDT is required for secretion of a protease in
Myxococcus xanthus
, suggesting that some TBDTs may be involved in protein secretion. |
doi_str_mv | 10.1038/s41467-019-09366-9 |
format | article |
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Myxococcus xanthus
is required for secretion of a protein, protease PopC, to the extracellular milieu. PopC accumulates in the periplasm before secretion across the outer membrane, and the proton motive force has a role in secretion to the extracellular milieu. Reconstitution experiments in
Escherichia coli
demonstrate that secretion of PopC across the outer membrane not only depends on Oar but also on the ExbB/ExbD/TonB system. Our results indicate that TBDTs and the ExbB/ExbD/TonB system may have roles not only in import processes but also in secretion of proteins.
TonB-dependent transporters (TBDTs) are outer membrane proteins that import nutrients and bacteriocins in bacteria. Here, Gómez-Santos et al. show that a TBDT is required for secretion of a protease in
Myxococcus xanthus
, suggesting that some TBDTs may be involved in protein secretion.</description><identifier>ISSN: 2041-1723</identifier><identifier>EISSN: 2041-1723</identifier><identifier>DOI: 10.1038/s41467-019-09366-9</identifier><identifier>PMID: 30911012</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>14/63 ; 38/1 ; 38/111 ; 38/70 ; 38/77 ; 38/88 ; 38/90 ; 42/70 ; 631/326 ; 631/45 ; 631/80/2023 ; 631/80/313 ; 631/80/313/2376 ; 82/58 ; 82/80 ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacteriocins ; Biological Transport ; Cell Membrane - metabolism ; E coli ; Escherichia coli - classification ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Gene Expression Regulation, Bacterial ; Genetic Complementation Test ; Humanities and Social Sciences ; Imports ; Isoenzymes - genetics ; Isoenzymes - metabolism ; Life Sciences ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; multidisciplinary ; Myxococcus xanthus ; Myxococcus xanthus - classification ; Myxococcus xanthus - genetics ; Myxococcus xanthus - metabolism ; Nutrients ; Peptide Hydrolases - genetics ; Peptide Hydrolases - metabolism ; Periplasm ; Periplasm - metabolism ; Phylogeny ; Protease ; Proteinase ; Proteins ; Proton-Motive Force ; Protonmotive force ; Protons ; Science ; Science (multidisciplinary) ; Secretion</subject><ispartof>Nature communications, 2019-03, Vol.10 (1), p.1360-1360, Article 1360</ispartof><rights>The Author(s) 2019</rights><rights>This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Attribution</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c640t-4b4c77e4ec3625871d599f78a61c1c5de56d19fe5a5511cf88742e3da42c1d1a3</citedby><cites>FETCH-LOGICAL-c640t-4b4c77e4ec3625871d599f78a61c1c5de56d19fe5a5511cf88742e3da42c1d1a3</cites><orcidid>0000-0002-1161-250X ; 0000-0002-0674-0013</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2197311521/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2197311521?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30911012$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-03626151$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Gómez-Santos, Nuria</creatorcontrib><creatorcontrib>Glatter, Timo</creatorcontrib><creatorcontrib>Koebnik, Ralf</creatorcontrib><creatorcontrib>Świątek-Połatyńska, Magdalena Anna</creatorcontrib><creatorcontrib>Søgaard-Andersen, Lotte</creatorcontrib><title>A TonB-dependent transporter is required for secretion of protease PopC across the bacterial outer membrane</title><title>Nature communications</title><addtitle>Nat Commun</addtitle><addtitle>Nat Commun</addtitle><description>TonB-dependent transporters (TBDTs) are ubiquitous outer membrane β-barrel proteins that import nutrients and bacteriocins across the outer membrane in a proton motive force-dependent manner, by directly connecting to the ExbB/ExbD/TonB system in the inner membrane. Here, we show that the TBDT Oar in
Myxococcus xanthus
is required for secretion of a protein, protease PopC, to the extracellular milieu. PopC accumulates in the periplasm before secretion across the outer membrane, and the proton motive force has a role in secretion to the extracellular milieu. Reconstitution experiments in
Escherichia coli
demonstrate that secretion of PopC across the outer membrane not only depends on Oar but also on the ExbB/ExbD/TonB system. Our results indicate that TBDTs and the ExbB/ExbD/TonB system may have roles not only in import processes but also in secretion of proteins.
TonB-dependent transporters (TBDTs) are outer membrane proteins that import nutrients and bacteriocins in bacteria. Here, Gómez-Santos et al. show that a TBDT is required for secretion of a protease in
Myxococcus xanthus
, suggesting that some TBDTs may be involved in protein secretion.</description><subject>14/63</subject><subject>38/1</subject><subject>38/111</subject><subject>38/70</subject><subject>38/77</subject><subject>38/88</subject><subject>38/90</subject><subject>42/70</subject><subject>631/326</subject><subject>631/45</subject><subject>631/80/2023</subject><subject>631/80/313</subject><subject>631/80/313/2376</subject><subject>82/58</subject><subject>82/80</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriocins</subject><subject>Biological Transport</subject><subject>Cell Membrane - metabolism</subject><subject>E coli</subject><subject>Escherichia coli - classification</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Genetic Complementation Test</subject><subject>Humanities and Social Sciences</subject><subject>Imports</subject><subject>Isoenzymes - 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Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Nature communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gómez-Santos, Nuria</au><au>Glatter, Timo</au><au>Koebnik, Ralf</au><au>Świątek-Połatyńska, Magdalena Anna</au><au>Søgaard-Andersen, Lotte</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A TonB-dependent transporter is required for secretion of protease PopC across the bacterial outer membrane</atitle><jtitle>Nature communications</jtitle><stitle>Nat Commun</stitle><addtitle>Nat Commun</addtitle><date>2019-03-25</date><risdate>2019</risdate><volume>10</volume><issue>1</issue><spage>1360</spage><epage>1360</epage><pages>1360-1360</pages><artnum>1360</artnum><issn>2041-1723</issn><eissn>2041-1723</eissn><abstract>TonB-dependent transporters (TBDTs) are ubiquitous outer membrane β-barrel proteins that import nutrients and bacteriocins across the outer membrane in a proton motive force-dependent manner, by directly connecting to the ExbB/ExbD/TonB system in the inner membrane. Here, we show that the TBDT Oar in
Myxococcus xanthus
is required for secretion of a protein, protease PopC, to the extracellular milieu. PopC accumulates in the periplasm before secretion across the outer membrane, and the proton motive force has a role in secretion to the extracellular milieu. Reconstitution experiments in
Escherichia coli
demonstrate that secretion of PopC across the outer membrane not only depends on Oar but also on the ExbB/ExbD/TonB system. Our results indicate that TBDTs and the ExbB/ExbD/TonB system may have roles not only in import processes but also in secretion of proteins.
TonB-dependent transporters (TBDTs) are outer membrane proteins that import nutrients and bacteriocins in bacteria. Here, Gómez-Santos et al. show that a TBDT is required for secretion of a protease in
Myxococcus xanthus
, suggesting that some TBDTs may be involved in protein secretion.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>30911012</pmid><doi>10.1038/s41467-019-09366-9</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-1161-250X</orcidid><orcidid>https://orcid.org/0000-0002-0674-0013</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | 14/63 38/1 38/111 38/70 38/77 38/88 38/90 42/70 631/326 631/45 631/80/2023 631/80/313 631/80/313/2376 82/58 82/80 Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriocins Biological Transport Cell Membrane - metabolism E coli Escherichia coli - classification Escherichia coli - genetics Escherichia coli - metabolism Gene Expression Regulation, Bacterial Genetic Complementation Test Humanities and Social Sciences Imports Isoenzymes - genetics Isoenzymes - metabolism Life Sciences Membrane Proteins - genetics Membrane Proteins - metabolism multidisciplinary Myxococcus xanthus Myxococcus xanthus - classification Myxococcus xanthus - genetics Myxococcus xanthus - metabolism Nutrients Peptide Hydrolases - genetics Peptide Hydrolases - metabolism Periplasm Periplasm - metabolism Phylogeny Protease Proteinase Proteins Proton-Motive Force Protonmotive force Protons Science Science (multidisciplinary) Secretion |
title | A TonB-dependent transporter is required for secretion of protease PopC across the bacterial outer membrane |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T18%3A59%3A44IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_doaj_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20TonB-dependent%20transporter%20is%20required%20for%20secretion%20of%20protease%20PopC%20across%20the%20bacterial%20outer%20membrane&rft.jtitle=Nature%20communications&rft.au=G%C3%B3mez-Santos,%20Nuria&rft.date=2019-03-25&rft.volume=10&rft.issue=1&rft.spage=1360&rft.epage=1360&rft.pages=1360-1360&rft.artnum=1360&rft.issn=2041-1723&rft.eissn=2041-1723&rft_id=info:doi/10.1038/s41467-019-09366-9&rft_dat=%3Cproquest_doaj_%3E2197899152%3C/proquest_doaj_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c640t-4b4c77e4ec3625871d599f78a61c1c5de56d19fe5a5511cf88742e3da42c1d1a3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2197311521&rft_id=info:pmid/30911012&rfr_iscdi=true |