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Quorum sensing is a chemical communication process that bacteria use to coordinate group behaviors.  Pseudomonas aeruginosa , an opportunistic pathogen, employs multiple quorum-sensing systems to control behaviors including virulence factor production and biofilm formation. One  P .  aeruginosa  quorum-sensing receptor, called RhlR, binds the cognate autoinducer  N -butryl-homoserine lactone (C 4 HSL), and the RhlR:C 4 HSL complex activates transcription of target quorum-sensing genes. Here, we use a genetic screen to identify RhlR mutants that function independently of the autoinducer. The RhlR Y64F W68F V133F triple mutant, which we call RhlR*, exhibits ligand-independent activity  in vitro  and  in vivo . RhlR* can drive wildtype biofilm formation and infection in a nematode animal model. The ability of RhlR* to properly regulate quorum-sensing-controlled genes  in vivo  depends on the quorum-sensing regulator RsaL keeping RhlR* activity in check. RhlR is known to function together with PqsE to control production of the virulence factor called pyocyanin. Likewise, RhlR* requires PqsE for pyocyanin production in planktonic cultures, however, PqsE is dispensable for RhlR*-driven pyocyanin production on surfaces. Finally, wildtype RhlR protein is not sufficiently stabilized by C 4 HSL to allow purification. However, wildtype RhlR can be stabilized by the synthetic ligand mBTL ( meta -bromo-thiolactone) and RhlR* is stable without a ligand. These features enabled purification of the RhlR:mBTL complex and of RhlR* for  in vitro  examination of their biochemical activities. To our knowledge, this work reports the first RhlR protein purification.

An autoinducer-independent RhlR quorum-sensing receptor enables analysis of RhlR regulation