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 AbstractFeeding a high-concentrate corn straw diet induced epigenetic alterations in the mammary tissue of dairy cows    Next AbstractIdentification and analysis of odor-active substances from PVC-overlaid MDF »

Sci Rep


Title:"Membrane Topology and Structural Insights into the Peptide Pheromone Receptor ComD, A Quorum-Sensing Histidine Protein Kinase of Streptococcus mutans"
Author(s):Dong G; Tian XL; Cyr K; Liu T; Lin W; Tziolas G; Li YH;
Address:"Department of Applied Oral Sciences 5981 University Ave, Halifax, NS, B3H 1W2, Canada. Department of Microbiology and Immunology, 5850 College Street, Halifax, NS, B3H 4R2, Canada"
Journal Title:Sci Rep
Year:2016
Volume:20160520
Issue:
Page Number:26502 -
DOI: 10.1038/srep26502
ISSN/ISBN:2045-2322 (Electronic) 2045-2322 (Linking)
Abstract:"Quorum sensing activation by signal pheromone (CSP) in Streptococcus mutans depends on the membrane-associated receptor ComD, which senses the signal and triggers the signaling cascade for bacteriocin production and other cell density-dependent activities. However, the mechanism of the signal recognition via the ComD receptor in this species is nearly unexplored. Here, we show that the membrane domain of the ComD protein forms six transmembrane segments with three extracellular loops, loopA, loopB and loopC. By structural and functional analyses of these extracellular loops, we demonstrate that both loopC and loopB are required for CSP recognition, while loopA plays little role in CSP detection. A deletion or substitution mutation of four residues NVIP in loopC abolishes CSP recognition for quorum sensing activities. We conclude that both loopC and loopB are required for forming the receptor and residues NVIP of loopC are essential for CSP recognition and quorum sensing activation in S. mutans"
Keywords:"Bacterial Proteins/chemistry/genetics/metabolism Cell Membrane/chemistry/metabolism Gene Expression Regulation, Bacterial Histidine Kinase/*chemistry/genetics/*metabolism Point Mutation Protein Conformation Quorum Sensing Streptococcus mutans/metabolism/*;"
Notes:"MedlineDong, Gaofeng Tian, Xiao-Lin Cyr, Kayla Liu, Tianlei Lin, William Tziolas, Geoffrey Li, Yung-Hua eng MOP-115007/CIHR/Canada Research Support, Non-U.S. Gov't England 2016/05/21 Sci Rep. 2016 May 20; 6:26502. doi: 10.1038/srep26502"

 
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 19-12-2024