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 AbstractThe role of the vomeronasal organ in behavioral control of reproduction    Next AbstractA predatory mechanism dramatically increases the efficiency of lateral gene transfer in Streptococcus pneumoniae and related commensal species »

J Bacteriol


Title:"Structural analysis of the peptide pheromone receptor PlnB, a histidine protein kinase from Lactobacillus plantarum"
Author(s):Johnsborg O; Diep DB; Nes IF;
Address:"Laboratory of Microbial Gene Technology, Department of Chemistry and Biotechnology, Agricultural University of Norway, N-1432 As, Norway. olav.johnsborg@ikb.nlh.no"
Journal Title:J Bacteriol
Year:2003
Volume:185
Issue:23
Page Number:6913 - 6920
DOI: 10.1128/JB.185.23.6913-6920.2003
ISSN/ISBN:0021-9193 (Print) 1098-5530 (Electronic) 0021-9193 (Linking)
Abstract:"Intercellular communication plays a key role in the regulation of several physiological processes in gram-positive bacteria. Cell-cell communication is often mediated by secreted inducer peptide pheromones (IPs), which upon reaching a threshold concentration in the environment specifically activate a cognate membrane-localized histidine protein kinase (HPK). Interestingly, the majority of IP-activated HPKs fall into one distinct subfamily (HPK(10)). As part of an effort to study the mechanism underlying pheromone-mediated activation of the HPK(10) subfamily, the present work investigated the membrane topology of PlnB from Lactobacillus plantarum. Gene fusion experiments with Escherichia coli and Lactobacillus sakei, using alkaline phosphatase, beta-lactamase, and beta-galactosidase reporter fusions, suggested that PlnB is anchored to the cytoplasmic membrane via seven transmembrane segments. By domain switching between HPK(10) members, it was demonstrated that the determinants for pheromone binding and specificity are contained within the transmembrane domain. The results also indicate that the mechanism of signal transduction, in which the final transmembrane segment apparently plays a key role, is conserved between members of the HPK(10) subfamily"
Keywords:"Amino Acid Sequence Enzyme Activation Genes, Bacterial Histidine Kinase Lactobacillus/*enzymology/metabolism Molecular Sequence Data Oligopeptides/metabolism Protein Binding Protein Kinases/chemistry/*genetics/metabolism Protein Structure, Secondary Recep;"
Notes:"MedlineJohnsborg, Ola Diep, Dzung B Nes, Ingolf F eng Research Support, Non-U.S. Gov't 2003/11/18 J Bacteriol. 2003 Dec; 185(23):6913-20. doi: 10.1128/JB.185.23.6913-6920.2003"

 
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 25-11-2024