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

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posted on 2018-01-25, 11:21 authored by James T. Hodgkinson, Jeremy Gross, Ysobel R. Baker, David R. Spring, M. Welch
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.

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Citation

Chemical Science, 2016, 7 (4), pp. 2553-2562

Author affiliation

/Organisation/COLLEGE OF SCIENCE AND ENGINEERING/Department of Chemistry

Version

  • VoR (Version of Record)

Published in

Chemical Science

Publisher

Royal Society of Chemistry

issn

2041-6520

eissn

2041-6539

Acceptance date

2016-01-08

Copyright date

2016

Available date

2018-01-25

Publisher version

http://pubs.rsc.org/en/Content/ArticleLanding/2016/SC/C5SC04197J#!divAbstract

Language

en

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