Corseting a tripartite ABC transporter to make it fit for transport
ABC transporters have long been known to mediate resistance phenotypes in all kingdoms of life, and ATP-driven tripartite efflux pump from Gram-negative bacteria have attracted increasing interest. We give a special focus on MacAB TolC, a prototypical member of the recently described Type VII ABC tr...
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| Veröffentlicht in: | Biochimie 2023-02, Vol.205, p.117-123 |
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| container_title | Biochimie |
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| creator | Batista dos Santos, William Souabni, Hager Picard, Martin |
| description | ABC transporters have long been known to mediate resistance phenotypes in all kingdoms of life, and ATP-driven tripartite efflux pump from Gram-negative bacteria have attracted increasing interest. We give a special focus on MacAB TolC, a prototypical member of the recently described Type VII ABC transporter superfamily, from Escherichia coli. We provide original experimental evidence for the in vitro, substrate-induced ATPase activity and show a maximal activity when the tripartite pump is fully assembled in lipid nanodiscs. These results are evaluated and interpreted in the context of the structural and functional data that have accumulated over the years.
•MacAB TolC shows maximal activity when fully assembled and reconstituted in lipids.•MacB is under strict dependance of the hydrophobic environment.•There is an intricate mutual interdependency among MacB, MacA and TolC.•The Periplasmic Core Domain plays a pivotal role in the functioning of the pump. |
| doi_str_mv | 10.1016/j.biochi.2022.11.012 |
| format | Article |
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•MacAB TolC shows maximal activity when fully assembled and reconstituted in lipids.•MacB is under strict dependance of the hydrophobic environment.•There is an intricate mutual interdependency among MacB, MacA and TolC.•The Periplasmic Core Domain plays a pivotal role in the functioning of the pump.</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/j.biochi.2022.11.012</identifier><identifier>PMID: 36442691</identifier><language>eng</language><publisher>France: Elsevier B.V</publisher><subject>ABC ; ABC transporters ; adenosinetriphosphatase ; ATP-Binding Cassette Transporters ; Bacterial Outer Membrane Proteins - chemistry ; Escherichia coli ; Escherichia coli - metabolism ; Escherichia coli Proteins - metabolism ; Life Sciences ; lipids ; Membrane protein ; Membrane Transport Proteins - chemistry ; Structure-function study ; superfamily ; Transport of drugs across membranes</subject><ispartof>Biochimie, 2023-02, Vol.205, p.117-123</ispartof><rights>2022</rights><rights>Copyright © 2022. Published by Elsevier B.V.</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-c475t-d5a9c7752ac11e85f7f843a473d7e28f3348c932458dc6bbd3bf34e4eb7e228e3</citedby><cites>FETCH-LOGICAL-c475t-d5a9c7752ac11e85f7f843a473d7e28f3348c932458dc6bbd3bf34e4eb7e228e3</cites><orcidid>0000-0002-6518-8900</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S030090842200308X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36442691$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://cnrs.hal.science/hal-04018543$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Batista dos Santos, William</creatorcontrib><creatorcontrib>Souabni, Hager</creatorcontrib><creatorcontrib>Picard, Martin</creatorcontrib><title>Corseting a tripartite ABC transporter to make it fit for transport</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>ABC transporters have long been known to mediate resistance phenotypes in all kingdoms of life, and ATP-driven tripartite efflux pump from Gram-negative bacteria have attracted increasing interest. We give a special focus on MacAB TolC, a prototypical member of the recently described Type VII ABC transporter superfamily, from Escherichia coli. We provide original experimental evidence for the in vitro, substrate-induced ATPase activity and show a maximal activity when the tripartite pump is fully assembled in lipid nanodiscs. These results are evaluated and interpreted in the context of the structural and functional data that have accumulated over the years.
•MacAB TolC shows maximal activity when fully assembled and reconstituted in lipids.•MacB is under strict dependance of the hydrophobic environment.•There is an intricate mutual interdependency among MacB, MacA and TolC.•The Periplasmic Core Domain plays a pivotal role in the functioning of the pump.</description><subject>ABC</subject><subject>ABC transporters</subject><subject>adenosinetriphosphatase</subject><subject>ATP-Binding Cassette Transporters</subject><subject>Bacterial Outer Membrane Proteins - chemistry</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Life Sciences</subject><subject>lipids</subject><subject>Membrane protein</subject><subject>Membrane Transport Proteins - chemistry</subject><subject>Structure-function study</subject><subject>superfamily</subject><subject>Transport of drugs across membranes</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1PGzEQQC0EgpTyDxDaIz3s4vHHrvdSKV21BSkSF3q2vN5Z4pDEqe1E6r-vowV6K4eRNZ43HmseIddAK6BQ362q3nm7dBWjjFUAFQV2QmZQc1XWoPgpmVFOadlSJS7IpxhXlFJJWXtOLngtBKtbmJGu8yFictvnwhQpuJ0JySUs5t-6nJpt3PmQMBTJFxvzgoVLxXgMH_6VP5Oz0awjXr2el-TXj-9P3X25ePz50M0XpRWNTOUgTWubRjJjAVDJsRmV4EY0fGiQqZFzoWzLmZBqsHXfD7wfuUCBfS4zhfySfJneXZq13gW3MeGP9sbp-_lCH--ooKCk4AfI7O3E7oL_vceY9MZFi-u12aLfR81BciXbumUfoqzJu5ItYyKjYkJt8DEGHN-_AVQfreiVnqzooxUNoLOV3HbzOmHfb3B4b3rTkIGvE4B5fQeHQUfrcGtxcAFt0oN3_5_wF984nXc</recordid><startdate>20230201</startdate><enddate>20230201</enddate><creator>Batista dos Santos, William</creator><creator>Souabni, Hager</creator><creator>Picard, Martin</creator><general>Elsevier B.V</general><general>Elsevier</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>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-6518-8900</orcidid></search><sort><creationdate>20230201</creationdate><title>Corseting a tripartite ABC transporter to make it fit for transport</title><author>Batista dos Santos, William ; Souabni, Hager ; Picard, Martin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c475t-d5a9c7752ac11e85f7f843a473d7e28f3348c932458dc6bbd3bf34e4eb7e228e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>ABC</topic><topic>ABC transporters</topic><topic>adenosinetriphosphatase</topic><topic>ATP-Binding Cassette Transporters</topic><topic>Bacterial Outer Membrane Proteins - chemistry</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Life Sciences</topic><topic>lipids</topic><topic>Membrane protein</topic><topic>Membrane Transport Proteins - chemistry</topic><topic>Structure-function study</topic><topic>superfamily</topic><topic>Transport of drugs across membranes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Batista dos Santos, William</creatorcontrib><creatorcontrib>Souabni, Hager</creatorcontrib><creatorcontrib>Picard, Martin</creatorcontrib><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>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Batista dos Santos, William</au><au>Souabni, Hager</au><au>Picard, Martin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Corseting a tripartite ABC transporter to make it fit for transport</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>2023-02-01</date><risdate>2023</risdate><volume>205</volume><spage>117</spage><epage>123</epage><pages>117-123</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><abstract>ABC transporters have long been known to mediate resistance phenotypes in all kingdoms of life, and ATP-driven tripartite efflux pump from Gram-negative bacteria have attracted increasing interest. We give a special focus on MacAB TolC, a prototypical member of the recently described Type VII ABC transporter superfamily, from Escherichia coli. We provide original experimental evidence for the in vitro, substrate-induced ATPase activity and show a maximal activity when the tripartite pump is fully assembled in lipid nanodiscs. These results are evaluated and interpreted in the context of the structural and functional data that have accumulated over the years.
•MacAB TolC shows maximal activity when fully assembled and reconstituted in lipids.•MacB is under strict dependance of the hydrophobic environment.•There is an intricate mutual interdependency among MacB, MacA and TolC.•The Periplasmic Core Domain plays a pivotal role in the functioning of the pump.</abstract><cop>France</cop><pub>Elsevier B.V</pub><pmid>36442691</pmid><doi>10.1016/j.biochi.2022.11.012</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-6518-8900</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochimie, 2023-02, Vol.205, p.117-123 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | ABC ABC transporters adenosinetriphosphatase ATP-Binding Cassette Transporters Bacterial Outer Membrane Proteins - chemistry Escherichia coli Escherichia coli - metabolism Escherichia coli Proteins - metabolism Life Sciences lipids Membrane protein Membrane Transport Proteins - chemistry Structure-function study superfamily Transport of drugs across membranes |
| title | Corseting a tripartite ABC transporter to make it fit for transport |
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