Autoinducer binding by the quorum-sensing regulator TraR increases affinity for target promoters in vitro and decreases TraR turnover rates in whole cells

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Abstract
TraR is an Agrobacterium transcriptional regulator whose activity requires the pheromone N-3-oxooctanoyl-l-homoserine lactone. TraR was purified as a complex with the pheromone and contained one pheromone molecule per protein monomer. TraR–pheromone complexes bound to a single DNA site and activated two promoters that flank this site. Promoter expression was elevated 30-fold by using a supercoiled template. Pheromone binding increased the affinity of TraR for this binding site. Pheromone also increased TraR abundance in vivo by causing a 20-fold decrease in TraR turnover rates.