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 AbstractAdvances in carbon isotope analysis of trapped methane and volatile hydrocarbons in crystalline rock cores    Next Abstract"Effect of Emulphor, an emulsifier, on the pharmacokinetics and hepatotoxicity of oral carbon tetrachloride in the rat" »

Arch Microbiol


Title:Genetic and functional characterization of dpp genes encoding a dipeptide transport system in Lactococcus lactis
Author(s):Sanz Y; Lanfermeijer FC; Renault P; Bolotin A; Konings WN; Poolman B;
Address:"Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands"
Journal Title:Arch Microbiol
Year:2001
Volume:175
Issue:5
Page Number:334 - 343
DOI: 10.1007/s002030100270
ISSN/ISBN:0302-8933 (Print) 0302-8933 (Linking)
Abstract:"The genes encoding a binding-protein-dependent ABC transporter for dipeptides (Dpp) were identified in Lactococcus lactis subsp. cremoris MG1363. Two (dppA and dppP) of the six ORFs (dppAdppPBCDF) encode proteins that are homologous to peptide- and pheromone-binding proteins. The dppP gene contains a chain-terminating nonsense mutation and a frame-shift that may impair its function. The functionality of the dpp genes was proven by the construction of disruption mutants via homologous recombination. The expression of DppA and various other components of the proteolytic system was studied in synthetic and peptide-rich media and by using isogenic peptide-transport mutants that are defective in one or more systems (Opp, DtpT, and/or Dpp). In peptide-rich medium, DppA was maximally expressed in mutants lacking Opp and DtpT. DppA expression also depended on the growth phase and was repressed by tri-leucine and tri-valine. The effect of tri-leucine on DppA expression was abolished when leucine was present in the medium. Importantly, the Dpp system also regulated the expression of other components of the proteolytic system. This regulation was achieved via the internalization of di-valine, which caused a 30-50% inhibition in the expression of the proteinase PrtP and the peptidases PepN and PepC. Similar to the regulation of DppA, the repressing effect was no longer observed when high concentrations of valine were present. The intricate regulation of the components of the proteolytic system by peptides and amino acids is discussed in the light of the new and published data"
Keywords:"Amino Acid Sequence Bacterial Proteins/genetics/metabolism Carrier Proteins/genetics/*metabolism Dipeptides/*metabolism Endopeptidases/metabolism *Escherichia coli Proteins Gene Expression Genes, Bacterial/*genetics Lactococcus lactis/*genetics/growth & d;"
Notes:"MedlineSanz, Y Lanfermeijer, F C Renault, P Bolotin, A Konings, W N Poolman, B eng Research Support, Non-U.S. Gov't Germany 2001/06/21 Arch Microbiol. 2001 May; 175(5):334-43. doi: 10.1007/s002030100270"

 
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 27-12-2024