Structural highlights
Publication Abstract from PubMed
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.
BrlR from Pseudomonas aeruginosa is a receptor for both cyclic di-GMP and pyocyanin.,Wang F, He Q, Yin J, Xu S, Hu W, Gu L Nat Commun. 2018 Jul 2;9(1):2563. doi: 10.1038/s41467-018-05004-y. PMID:29967320[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang F, He Q, Yin J, Xu S, Hu W, Gu L. BrlR from Pseudomonas aeruginosa is a receptor for both cyclic di-GMP and pyocyanin. Nat Commun. 2018 Jul 2;9(1):2563. doi: 10.1038/s41467-018-05004-y. PMID:29967320 doi:http://dx.doi.org/10.1038/s41467-018-05004-y
