Issue 4, 2016
From the journal:

Chemical Science

A new Pseudomonas quinolone signal (PQS) binding partner: MexG†

James T. Hodgkinson,a   Jeremy Gross,b   Ysobel R. Baker,a   David R. Springa  and  M. Welch ORCID logo *b  

* Corresponding authors

a Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, UK

b Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, UK
E-mail: mw240@cam.ac.uk

Abstract

The opportunistic pathogen Pseudomonas aeruginosa utilises the cell–cell signalling mechanism known as quorum sensing to regulate virulence. P. aeruginosa produces two quinolone-based quorum sensing signalling molecules; the Pseudomonas quinolone signal (PQS) and its biosynthetic precursor 2-heptyl-4(1H)-quinolone (HHQ). To date, only one receptor (the PqsR protein) has been identified that is capable of binding PQS and HHQ. Here, we report on the synthesis of PQS and HHQ affinity probes for chemical proteomic studies. The PQS affinity probe very effectively captured PqsR in vitro. In addition, we also identified an interaction between PQS and the “orphan” RND efflux pump protein, MexG. The PQS–MexG interaction was further confirmed by purifying MexG and characterizing its ability to bind PQS and HHQ in vitro. Our findings suggest that PQS may have multiple binding partners in the cell and provide important new tools for studying quinolone signalling in P. aeruginosa and other organisms.

Graphical abstract: A new Pseudomonas quinolone signal (PQS) binding partner: MexG

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Article information

DOI
https://doi.org/10.1039/C5SC04197J
Article type
Edge Article
Submitted
04 Nov 2015
Accepted
08 Jan 2016
First published
20 Jan 2016
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2016,7, 2553-2562

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A new Pseudomonas quinolone signal (PQS) binding partner: MexG

J. T. Hodgkinson, J. Gross, Y. R. Baker, D. R. Spring and M. Welch, Chem. Sci., 2016, 7, 2553 DOI: 10.1039/C5SC04197J

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