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Tripartite assembly of RND multidrug efflux pumps

dc.contributor.authorDAURY, Laetitia
dc.contributor.authorORANGE, Francois
dc.contributor.authorTAVEAU, Jean-Christophe
dc.contributor.authorVERCHERE, Alice
dc.contributor.authorMONLEZUN, Laura
dc.contributor.authorGOUNOU, Celine
dc.contributor.authorMARREDDY, Ravi K. R.
dc.contributor.authorPICARD, Martin
dc.contributor.authorBROUTIN, Isabelle
dc.contributor.authorPOS, Klaas M.
dc.contributor.authorLAMBERT, Olivier
dc.date.accessioned2020-09-03T07:56:22Z
dc.date.available2020-09-03T07:56:22Z
dc.date.issued2016
dc.identifier.issn2041-1723
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10884
dc.description.abstractEnTripartite multidrug efflux systems of Gram-negative bacteria are composed of an inner membrane transporter, an outer membrane channel and a periplasmic adaptor protein. They are assumed to form ducts inside the periplasm facilitating drug exit across the outer membrane. Here we present the reconstitution of native Pseudomonas aeruginosa MexAB-OprM and Escherichia coli AcrAB-TolC tripartite Resistance Nodulation and cell Division (RND) efflux systems in a lipid nanodisc system. Single-particle analysis by electron microscopy reveals the inner and outer membrane protein components linked together via the periplasmic adaptor protein. This intrinsic ability of the native components to self-assemble also leads to the formation of a stable interspecies AcrA-MexB-TolC complex suggesting a common mechanism of tripartite assembly. Projection structures of all three complexes emphasize the role of the periplasmic adaptor protein as part of the exit duct with no physical interaction between the inner and outer membrane components.
dc.language.isoen
dc.title.enTripartite assembly of RND multidrug efflux pumps
dc.typeArticle de revue
dc.identifier.doi10.1038/ncomms10731
dc.subject.halChimie/Matériaux
bordeaux.journalNature Communications
bordeaux.volume7
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Nature%20Communications&rft.date=2016&rft.volume=7&rft.eissn=2041-1723&rft.issn=2041-1723&rft.au=DAURY,%20Laetitia&ORANGE,%20Francois&TAVEAU,%20Jean-Christophe&VERCHERE,%20Alice&MONLEZUN,%20Laura&rft.genre=article


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