Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous Abstract"Fine structure and function of the coxal glands of lithobiomorph centipedes: Lithobius forficatus and L. crassipes (Chilopoda, Lithobiidae)"    Next AbstractFemale scent signals enhance the resistance of male mice to influenza »

FEBS Lett


Title:The gelatinase biosynthesis-activating pheromone binds and stabilises the FsrB membrane protein in Enterococcus faecalis quorum sensing
Author(s):Littlewood S; Tattersall H; Hughes CS; Hussain R; Ma P; Harding SE; Nakayama J; Phillips-Jones MK;
Address:"School of Pharmacy and Biomedical Sciences, University of Central Lancashire, Preston, UK. Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, UK. Astbury Centre for Structural Molecular Biology, University of Leeds, UK. National Centre for Macromolecular Hydrodynamics, School of Biosciences, University of Nottingham, Sutton Bonington, UK. Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka, Japan"
Journal Title:FEBS Lett
Year:2020
Volume:20191021
Issue:3
Page Number:553 - 563
DOI: 10.1002/1873-3468.13634
ISSN/ISBN:1873-3468 (Electronic) 0014-5793 (Print) 0014-5793 (Linking)
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 CD measurements demonstrated a predominantly alpha-helical protein exhibiting a small level of conformational flexibility. Fivefold (400 mum) GBAP stabilised FsrB (80 mum) secondary structure. FsrB thermal denaturation in the presence and absence of GBAP revealed melting temperatures of 70.1 and 60.8 degrees C, respectively, demonstrating GBAP interactions and increased thermal stability conferred by GBAP. Addition of GBAP also resulted in tertiary structural changes, confirming GBAP binding"
Keywords:"Amino Acid Sequence Bacterial Proteins/chemistry/*metabolism Enterococcus faecalis/*cytology/drug effects/*metabolism Lactones/*metabolism/*pharmacology Peptides, Cyclic/*metabolism/*pharmacology Protein Binding Protein Conformation, alpha-Helical Protein;"
Notes:"MedlineLittlewood, Sean Tattersall, Helena Hughes, Charlotte S Hussain, Rohanah Ma, Pikyee Harding, Stephen E Nakayama, Jiro Phillips-Jones, Mary K eng BB/D001641/1/BB_/Biotechnology and Biological Sciences Research Council/United Kingdom Research Support, Non-U.S. Gov't England 2019/10/11 FEBS Lett. 2020 Feb; 594(3):553-563. doi: 10.1002/1873-3468.13634. Epub 2019 Oct 21"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 12-12-2024