The structure of BrlR reveals a potential pyocyanin binding site

Abstract

The transcriptional regulator BrlR from Pseudomonas aeruginosa is a member of the MerR family of multidrug transport activators. Studies have shown that BrlR plays an important role in the drug tolerance of P. aeruginosa in biofilms. The tolerance to drugs can be enhanced by 3',5'-cyclic diguanylic acid (c-di-GMP). In the present study, we analyze the apo structure of BrlR and the direct binding between GyrI-like domain of BrlR and P. aeruginosa toxin pyocyanin. Furthermore, we show that pyocyanin can enhance the binding between BrlR and DNA in vitro. These findings suggest that BrlR can serve as the binding partner for both c-di-GMP and pyocyanin.

Keywords: Pseudomonas aeruginosa; BrlR; cyclic diguanylic acid; pyocyanin.