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

AUTOR(ES)
FONTE

The National Academy of Sciences

RESUMO

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.

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