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The Gelatinase Biosynthesis‐Activating Pheromone binds and stabilizes the FsrB membrane protein in Enterococcus faecalis quorum sensing

DOI: 10.1002/1873-3468.13634 DOI Help

Authors: Sean Littlewood (University of Central Lancashire) , Helena Tattersall (University of Central Lancashire) , Charlotte S. Hughes (University of Central Lancashire; Diamond Light Source) , Rohanah Hussain (Diamond Light Source) , Pikyee Ma (University of Leeds) , Stephen E. Harding (University of Nottingham) , Jiro Nakayama (Kyushu University) , Mary Phillips-jones (University of Nottingham)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters

State: Published (Approved)
Published: October 2019
Diamond Proposal Number(s): 10310

Open Access Open Access

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.

Journal Keywords: FsrB; quorum sensing; Enterococcus faecalis; circular dichroism

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: B23-Circular Dichroism