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

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

SUBMITTER: Hodgkinson JT 

PROVIDER: S-EPMC5477026 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature