Tripartite assembly of RND multidrug efflux pumps

Laetitia Daury, François Orange, Jean-Christophe Taveau, Alice Verchère, Laura Monlezun, Céline Gounou, Ravi K. R. Marreddy, Martin Picard, Isabelle Broutin, Klaas M. Pos and Olivier Lambert ()
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Laetitia Daury: Université de Bordeaux, CBMN UMR 5248, Bordeaux INP, IECB
François Orange: Université de Bordeaux, CBMN UMR 5248, Bordeaux INP, IECB
Jean-Christophe Taveau: Université de Bordeaux, CBMN UMR 5248, Bordeaux INP, IECB
Alice Verchère: Laboratoire de Cristallographie et RMN Biologiques, UMR 8015, CNRS, Université Paris Descartes, Faculté de Pharmacie
Laura Monlezun: Laboratoire de Cristallographie et RMN Biologiques, UMR 8015, CNRS, Université Paris Descartes, Faculté de Pharmacie
Céline Gounou: Université de Bordeaux, CBMN UMR 5248, Bordeaux INP, IECB
Ravi K. R. Marreddy: Institute of Biochemistry, Goethe-University Frankfurt
Martin Picard: Laboratoire de Cristallographie et RMN Biologiques, UMR 8015, CNRS, Université Paris Descartes, Faculté de Pharmacie
Isabelle Broutin: Laboratoire de Cristallographie et RMN Biologiques, UMR 8015, CNRS, Université Paris Descartes, Faculté de Pharmacie
Klaas M. Pos: Institute of Biochemistry, Goethe-University Frankfurt
Olivier Lambert: Université de Bordeaux, CBMN UMR 5248, Bordeaux INP, IECB

Nature Communications, 2016, vol. 7, issue 1, 1-8

Abstract: Abstract Tripartite 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.

Date: 2016
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DOI: 10.1038/ncomms10731

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