The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism
Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol...
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creator | Szczepaniak, Joanna Holmes, Peter Rajasekar, Karthik Kaminska, Renata Samsudin, Firdaus Inns, Patrick George Rassam, Patrice Khalid, Syma Murray, Seán M. Redfield, Christina Kleanthous, Colin |
description | Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol system. Here, we show that Pal accumulation at
Escherichia coli
division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system.
The lipoprotein Pal participates in the coordination of outer-membrane constriction with septation in Gram-negative bacteria. Here, the authors show that this coordination is mediated by active mobilisation-and-capture of Pal at division septa by the Tol system. |
doi_str_mv | 10.1038/s41467-020-15083-5 |
format | Article |
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Escherichia coli
division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system.
The lipoprotein Pal participates in the coordination of outer-membrane constriction with septation in Gram-negative bacteria. Here, the authors show that this coordination is mediated by active mobilisation-and-capture of Pal at division septa by the Tol system.</description><identifier>ISSN: 2041-1723</identifier><identifier>EISSN: 2041-1723</identifier><identifier>DOI: 10.1038/s41467-020-15083-5</identifier><identifier>PMID: 32161270</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>101/6 ; 14/19 ; 14/35 ; 14/63 ; 631/326/41/2536 ; 631/326/88 ; 631/45/612/1191 ; 82/1 ; 82/80 ; Bacteria ; Bacterial Outer Membrane - metabolism ; Bacterial Outer Membrane Proteins - metabolism ; Binding ; Biochemistry, Molecular Biology ; Cell Division ; Cell walls ; Constrictions ; Coordination ; E coli ; Escherichia coli - cytology ; Escherichia coli - metabolism ; Escherichia coli Proteins - metabolism ; Gram-negative bacteria ; Humanities and Social Sciences ; Life Sciences ; Lipoproteins ; Lipoproteins - metabolism ; Membrane Proteins ; Membranes ; multidisciplinary ; Peptidoglycan - metabolism ; Peptidoglycans ; Periplasmic Proteins - metabolism ; Science ; Science (multidisciplinary) ; Septation ; Septum</subject><ispartof>Nature communications, 2020-03, Vol.11 (1), p.1305-1305, Article 1305</ispartof><rights>The Author(s) 2020</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>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-c574t-61b7b7fa1af134d4f6effb46a82041f96c12f21f7c9adc7d4b73eec98fc2485e3</citedby><cites>FETCH-LOGICAL-c574t-61b7b7fa1af134d4f6effb46a82041f96c12f21f7c9adc7d4b73eec98fc2485e3</cites><orcidid>0000-0002-2260-0774 ; 0000-0001-7297-7708 ; 0000-0002-3273-0302 ; 0000-0003-2441-6310</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7066135/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7066135/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,27924,27925,41120,42189,51576,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32161270$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-03871449$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Szczepaniak, Joanna</creatorcontrib><creatorcontrib>Holmes, Peter</creatorcontrib><creatorcontrib>Rajasekar, Karthik</creatorcontrib><creatorcontrib>Kaminska, Renata</creatorcontrib><creatorcontrib>Samsudin, Firdaus</creatorcontrib><creatorcontrib>Inns, Patrick George</creatorcontrib><creatorcontrib>Rassam, Patrice</creatorcontrib><creatorcontrib>Khalid, Syma</creatorcontrib><creatorcontrib>Murray, Seán M.</creatorcontrib><creatorcontrib>Redfield, Christina</creatorcontrib><creatorcontrib>Kleanthous, Colin</creatorcontrib><title>The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism</title><title>Nature communications</title><addtitle>Nat Commun</addtitle><addtitle>Nat Commun</addtitle><description>Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol system. Here, we show that Pal accumulation at
Escherichia coli
division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system.
The lipoprotein Pal participates in the coordination of outer-membrane constriction with septation in Gram-negative bacteria. Here, the authors show that this coordination is mediated by active mobilisation-and-capture of Pal at division septa by the Tol system.</description><subject>101/6</subject><subject>14/19</subject><subject>14/35</subject><subject>14/63</subject><subject>631/326/41/2536</subject><subject>631/326/88</subject><subject>631/45/612/1191</subject><subject>82/1</subject><subject>82/80</subject><subject>Bacteria</subject><subject>Bacterial Outer Membrane - metabolism</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Binding</subject><subject>Biochemistry, Molecular Biology</subject><subject>Cell Division</subject><subject>Cell walls</subject><subject>Constrictions</subject><subject>Coordination</subject><subject>E coli</subject><subject>Escherichia coli - cytology</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Gram-negative bacteria</subject><subject>Humanities and Social Sciences</subject><subject>Life Sciences</subject><subject>Lipoproteins</subject><subject>Lipoproteins - 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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>Szczepaniak, Joanna</au><au>Holmes, Peter</au><au>Rajasekar, Karthik</au><au>Kaminska, Renata</au><au>Samsudin, Firdaus</au><au>Inns, Patrick George</au><au>Rassam, Patrice</au><au>Khalid, Syma</au><au>Murray, Seán M.</au><au>Redfield, Christina</au><au>Kleanthous, Colin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism</atitle><jtitle>Nature communications</jtitle><stitle>Nat Commun</stitle><addtitle>Nat Commun</addtitle><date>2020-03-11</date><risdate>2020</risdate><volume>11</volume><issue>1</issue><spage>1305</spage><epage>1305</epage><pages>1305-1305</pages><artnum>1305</artnum><issn>2041-1723</issn><eissn>2041-1723</eissn><abstract>Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol system. Here, we show that Pal accumulation at
Escherichia coli
division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system.
The lipoprotein Pal participates in the coordination of outer-membrane constriction with septation in Gram-negative bacteria. Here, the authors show that this coordination is mediated by active mobilisation-and-capture of Pal at division septa by the Tol system.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>32161270</pmid><doi>10.1038/s41467-020-15083-5</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-2260-0774</orcidid><orcidid>https://orcid.org/0000-0001-7297-7708</orcidid><orcidid>https://orcid.org/0000-0002-3273-0302</orcidid><orcidid>https://orcid.org/0000-0003-2441-6310</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | 101/6 14/19 14/35 14/63 631/326/41/2536 631/326/88 631/45/612/1191 82/1 82/80 Bacteria Bacterial Outer Membrane - metabolism Bacterial Outer Membrane Proteins - metabolism Binding Biochemistry, Molecular Biology Cell Division Cell walls Constrictions Coordination E coli Escherichia coli - cytology Escherichia coli - metabolism Escherichia coli Proteins - metabolism Gram-negative bacteria Humanities and Social Sciences Life Sciences Lipoproteins Lipoproteins - metabolism Membrane Proteins Membranes multidisciplinary Peptidoglycan - metabolism Peptidoglycans Periplasmic Proteins - metabolism Science Science (multidisciplinary) Septation Septum |
title | The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism |
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