Dissection of an ABC transporter LolCDE function analyzed by photo-crosslinking
Abstract The envelope of Escherichia coli contains approximately 100 different species of lipoproteins, most of which are localized to the inner leaflet of the outer membrane. The localization of lipoprotein (Lol) system, consisting of five Lol proteins, is responsible for the trafficking of lipopro...
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Veröffentlicht in: | Journal of biochemistry (Tokyo) 2024-03, Vol.175 (4), p.427-437 |
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creator | Tao, Kazuyuki Narita, Shin-ichiro Okada, Ui Murakami, Satoshi Tokuda, Hajime |
description | Abstract
The envelope of Escherichia coli contains approximately 100 different species of lipoproteins, most of which are localized to the inner leaflet of the outer membrane. The localization of lipoprotein (Lol) system, consisting of five Lol proteins, is responsible for the trafficking of lipoproteins to the outer membrane. LolCDE binds to lipoproteins destined for the outer membrane and transfers them to the periplasmic chaperone LolA. Although the cryo-EM structures of E. coli LolCDE have been reported, the mechanisms by which outer membrane lipoproteins are transferred to LolA remain elusive. In this study, we investigated the interaction between LolCDE and lipoproteins using site-specific photo-crosslinking. We introduced a photo-crosslinkable amino acid into different locations across the four helices which form the central lipoprotein-binding cavity, and identified domains that crosslink with peptidoglycan-associated lipoprotein (Pal) in vivo. Using one of the derivatives containing the photo-crosslinkable amino acid, we developed an in vitro system to analyze the binding of lipoproteins to LolCDE. Our results indicate that compound 2, a LolCDE inhibitor, does not inhibit the binding of lipoproteins to LolCDE, but rather promotes the dissociation of bound lipoproteins from LolCDE.
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doi_str_mv | 10.1093/jb/mvad118 |
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The envelope of Escherichia coli contains approximately 100 different species of lipoproteins, most of which are localized to the inner leaflet of the outer membrane. The localization of lipoprotein (Lol) system, consisting of five Lol proteins, is responsible for the trafficking of lipoproteins to the outer membrane. LolCDE binds to lipoproteins destined for the outer membrane and transfers them to the periplasmic chaperone LolA. Although the cryo-EM structures of E. coli LolCDE have been reported, the mechanisms by which outer membrane lipoproteins are transferred to LolA remain elusive. In this study, we investigated the interaction between LolCDE and lipoproteins using site-specific photo-crosslinking. We introduced a photo-crosslinkable amino acid into different locations across the four helices which form the central lipoprotein-binding cavity, and identified domains that crosslink with peptidoglycan-associated lipoprotein (Pal) in vivo. Using one of the derivatives containing the photo-crosslinkable amino acid, we developed an in vitro system to analyze the binding of lipoproteins to LolCDE. Our results indicate that compound 2, a LolCDE inhibitor, does not inhibit the binding of lipoproteins to LolCDE, but rather promotes the dissociation of bound lipoproteins from LolCDE.
Graphical Abstract
Graphical Abstract</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/jb/mvad118</identifier><identifier>PMID: 38156779</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Amino Acids - metabolism ; ATP-Binding Cassette Transporters - metabolism ; Bacterial Outer Membrane Proteins - metabolism ; Cell Membrane - metabolism ; Escherichia coli - metabolism ; Escherichia coli Proteins - metabolism ; Lipoproteins - chemistry ; Lipoproteins - metabolism ; Periplasmic Binding Proteins - metabolism ; Regular Paper</subject><ispartof>Journal of biochemistry (Tokyo), 2024-03, Vol.175 (4), p.427-437</ispartof><rights>The Author(s) 2024. Published by Oxford University Press on behalf of the Japanese Biochemical Society. 2024</rights><rights>The Author(s) 2024. Published by Oxford University Press on behalf of the Japanese Biochemical Society.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c439t-fcc118d6ffb7ea4ac4dac870b2705c0249a1d29837e384cd0ebe7e9ad3be2e263</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,1578,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38156779$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tao, Kazuyuki</creatorcontrib><creatorcontrib>Narita, Shin-ichiro</creatorcontrib><creatorcontrib>Okada, Ui</creatorcontrib><creatorcontrib>Murakami, Satoshi</creatorcontrib><creatorcontrib>Tokuda, Hajime</creatorcontrib><title>Dissection of an ABC transporter LolCDE function analyzed by photo-crosslinking</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>Abstract
The envelope of Escherichia coli contains approximately 100 different species of lipoproteins, most of which are localized to the inner leaflet of the outer membrane. The localization of lipoprotein (Lol) system, consisting of five Lol proteins, is responsible for the trafficking of lipoproteins to the outer membrane. LolCDE binds to lipoproteins destined for the outer membrane and transfers them to the periplasmic chaperone LolA. Although the cryo-EM structures of E. coli LolCDE have been reported, the mechanisms by which outer membrane lipoproteins are transferred to LolA remain elusive. In this study, we investigated the interaction between LolCDE and lipoproteins using site-specific photo-crosslinking. We introduced a photo-crosslinkable amino acid into different locations across the four helices which form the central lipoprotein-binding cavity, and identified domains that crosslink with peptidoglycan-associated lipoprotein (Pal) in vivo. Using one of the derivatives containing the photo-crosslinkable amino acid, we developed an in vitro system to analyze the binding of lipoproteins to LolCDE. Our results indicate that compound 2, a LolCDE inhibitor, does not inhibit the binding of lipoproteins to LolCDE, but rather promotes the dissociation of bound lipoproteins from LolCDE.
Graphical Abstract
Graphical Abstract</description><subject>Amino Acids - metabolism</subject><subject>ATP-Binding Cassette Transporters - metabolism</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Lipoproteins - chemistry</subject><subject>Lipoproteins - metabolism</subject><subject>Periplasmic Binding Proteins - metabolism</subject><subject>Regular Paper</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>TOX</sourceid><sourceid>EIF</sourceid><recordid>eNp9kU1Lw0AQhhdRbK1e_AGSiyBC7H7lY09S0_oBhV4UvC2bzaRNTXdjNinUX29qq-jF0zDMwzvvzIvQOcE3BAs2XKbD1VplhMQHqE-iIPRpGJBD1MeYEl9Q_tpDJ84tty1l7Bj1WEyCMIpEH83GhXOgm8Iaz-aeMt7oLvGaWhlX2bqB2pvaMhlPvLw1O0oZVW4-IPPSjVctbGN9XVvnysK8FWZ-io5yVTo429cBermfPCeP_nT28JSMpr7mTDR-rnVnNwvzPI1AcaV5pnQc4ZRGONCYcqFIRkXMImAx1xmGFCIQKmMpUKAhG6DbnW7VpivINJjOcymrulipeiOtKuTfiSkWcm7XkhCMAyF4p3C1V6jtewuukavCaShLZcC2TlKBBY45x0GHXu_Qr0tryH_2ECy3EchlKvcRdPDFb2c_6PfPO-ByB9i2-k_oE0BGkaY</recordid><startdate>20240325</startdate><enddate>20240325</enddate><creator>Tao, Kazuyuki</creator><creator>Narita, Shin-ichiro</creator><creator>Okada, Ui</creator><creator>Murakami, Satoshi</creator><creator>Tokuda, Hajime</creator><general>Oxford University Press</general><scope>TOX</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><scope>5PM</scope></search><sort><creationdate>20240325</creationdate><title>Dissection of an ABC transporter LolCDE function analyzed by photo-crosslinking</title><author>Tao, Kazuyuki ; Narita, Shin-ichiro ; Okada, Ui ; Murakami, Satoshi ; Tokuda, Hajime</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-fcc118d6ffb7ea4ac4dac870b2705c0249a1d29837e384cd0ebe7e9ad3be2e263</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Amino Acids - metabolism</topic><topic>ATP-Binding Cassette Transporters - metabolism</topic><topic>Bacterial Outer Membrane Proteins - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Lipoproteins - chemistry</topic><topic>Lipoproteins - metabolism</topic><topic>Periplasmic Binding Proteins - metabolism</topic><topic>Regular Paper</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tao, Kazuyuki</creatorcontrib><creatorcontrib>Narita, Shin-ichiro</creatorcontrib><creatorcontrib>Okada, Ui</creatorcontrib><creatorcontrib>Murakami, Satoshi</creatorcontrib><creatorcontrib>Tokuda, Hajime</creatorcontrib><collection>Oxford Journals Open Access Collection</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tao, Kazuyuki</au><au>Narita, Shin-ichiro</au><au>Okada, Ui</au><au>Murakami, Satoshi</au><au>Tokuda, Hajime</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dissection of an ABC transporter LolCDE function analyzed by photo-crosslinking</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>2024-03-25</date><risdate>2024</risdate><volume>175</volume><issue>4</issue><spage>427</spage><epage>437</epage><pages>427-437</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>Abstract
The envelope of Escherichia coli contains approximately 100 different species of lipoproteins, most of which are localized to the inner leaflet of the outer membrane. The localization of lipoprotein (Lol) system, consisting of five Lol proteins, is responsible for the trafficking of lipoproteins to the outer membrane. LolCDE binds to lipoproteins destined for the outer membrane and transfers them to the periplasmic chaperone LolA. Although the cryo-EM structures of E. coli LolCDE have been reported, the mechanisms by which outer membrane lipoproteins are transferred to LolA remain elusive. In this study, we investigated the interaction between LolCDE and lipoproteins using site-specific photo-crosslinking. We introduced a photo-crosslinkable amino acid into different locations across the four helices which form the central lipoprotein-binding cavity, and identified domains that crosslink with peptidoglycan-associated lipoprotein (Pal) in vivo. Using one of the derivatives containing the photo-crosslinkable amino acid, we developed an in vitro system to analyze the binding of lipoproteins to LolCDE. Our results indicate that compound 2, a LolCDE inhibitor, does not inhibit the binding of lipoproteins to LolCDE, but rather promotes the dissociation of bound lipoproteins from LolCDE.
Graphical Abstract
Graphical Abstract</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>38156779</pmid><doi>10.1093/jb/mvad118</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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source | Oxford University Press Journals All Titles (1996-Current); MEDLINE |
subjects | Amino Acids - metabolism ATP-Binding Cassette Transporters - metabolism Bacterial Outer Membrane Proteins - metabolism Cell Membrane - metabolism Escherichia coli - metabolism Escherichia coli Proteins - metabolism Lipoproteins - chemistry Lipoproteins - metabolism Periplasmic Binding Proteins - metabolism Regular Paper |
title | Dissection of an ABC transporter LolCDE function analyzed by photo-crosslinking |
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