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
Download full text from publisher
Corrections
All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10731. See general information about how to correct material in RePEc.
If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.
We have no bibliographic references for this item. You can help adding them by using this form .
If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.
For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .
Please note that corrections may take a couple of weeks to filter through
the various RePEc services.