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Tripartite assembly of RND multidrug efflux pumps

Author

Listed:
  • Laetitia Daury

    (Université de Bordeaux, CBMN UMR 5248, Bordeaux INP, IECB
    CNRS, CBMN UMR 5248)

  • François Orange

    (Université de Bordeaux, CBMN UMR 5248, Bordeaux INP, IECB
    CNRS, CBMN UMR 5248)

  • Jean-Christophe Taveau

    (Université de Bordeaux, CBMN UMR 5248, Bordeaux INP, IECB
    CNRS, CBMN UMR 5248)

  • 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
    CNRS, CBMN UMR 5248)

  • 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
    CNRS, CBMN UMR 5248)

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.

Suggested Citation

  • Laetitia Daury & François Orange & Jean-Christophe Taveau & Alice Verchère & Laura Monlezun & Céline Gounou & Ravi K. R. Marreddy & Martin Picard & Isabelle Broutin & Klaas M. Pos & Olivier Lambert, 2016. "Tripartite assembly of RND multidrug efflux pumps," Nature Communications, Nature, vol. 7(1), pages 1-8, April.
  • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10731
    DOI: 10.1038/ncomms10731
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    Cited by:

    1. Coline Plé & Heng-Keat Tam & Anais Vieira Da Cruz & Nina Compagne & Juan-Carlos Jiménez-Castellanos & Reinke T. Müller & Elizabeth Pradel & Wuen Ee Foong & Giuliano Malloci & Alexia Ballée & Moritz A., 2022. "Pyridylpiperazine-based allosteric inhibitors of RND-type multidrug efflux pumps," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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