BrlR from Pseudomonas aeruginosa is a receptor for both cyclic di-GMP and pyocyanin

Feng Wang, Qing He, Jia Yin, Sujuan Xu, Wei Hu () and Lichuan Gu ()
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Feng Wang: Shandong University
Qing He: Shandong University
Jia Yin: Shandong University
Sujuan Xu: Shandong University
Wei Hu: Shandong University
Lichuan Gu: Shandong University

Nature Communications, 2018, vol. 9, issue 1, 1-14

Abstract: Abstract The virulence factor pyocyanin and the intracellular second messenger cyclic diguanylate monophosphate (c-di-GMP) play key roles in regulating biofilm formation and multi-drug efflux pump expression in Pseudomonas aeruginosa. However, the crosstalk between these two signaling pathways remains unclear. Here we show that BrlR (PA4878), previously identified as a c-di-GMP responsive transcriptional regulator, acts also as a receptor for pyocyanin. Crystal structures of free BrlR and c-di-GMP-bound BrlR reveal that the DNA-binding domain of BrlR contains two separate c-di-GMP binding sites, both of which are involved in promoting brlR expression. In addition, we identify a pyocyanin-binding site on the C-terminal multidrug-binding domain based on the structure of the BrlR-C domain in complex with a pyocyanin analog. Biochemical analysis indicates that pyocyanin enhances BrlR-DNA binding and brlR expression in a concentration-dependent manner.

Date: 2018
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DOI: 10.1038/s41467-018-05004-y

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