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B23-Circular Dichroism	The gelatinase biosynthesis-activating pheromone binds and stabilises the FsrB membrane protein in Enterococcus faecalis quorum sensing Sean Littlewood , Helena Tattersall , Charlotte S. Hughes , Rohanah Hussain , Pikyee Ma , Stephen E. Harding , Jiro Nakayama , Mary Phillips-Jones Febs Letters DOI: 10.1002/1873-3468.13634 Diamond Proposal Number(s): [10310] Open Access Show Abstract ▼ Abstract: Quorum sensing mechanisms regulate gene expression in response to changing cell‐population density detected through pheromones. In Enterococcus faecalis, Fsr quorum sensing produces and responds to the gelatinase biosynthesis‐activating pheromone (GBAP). Here, we establish that the enterococcal FsrB membrane protein has a direct role connected with GBAP by showing that GBAP binds to purified FsrB. Far‐UV circular dichroism measurements demonstrated a predominantly α‐helical protein exhibiting a small level of conformational flexibility. Five‐fold (400 µM) GBAP stabilised FsrB (80 µM) secondary structure. FsrB thermal denaturation in the presence and absence of GBAP revealed melting temperatures of 70.1°C and 60.8°C respectively, demonstrating GBAP interactions and increased thermal stability conferred by GBAP. Addition of GBAP also resulted in tertiary structural changes, confirming GBAP binding.	Oct 2019

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