The signaling peptide NprX controlling ...
Document type :
Article dans une revue scientifique: Article original
DOI :
Permalink :
Title :
The signaling peptide NprX controlling sporulation and necrotrophism is imported intoBacillus thuringiensisby two oligopeptide permease systems
Author(s) :
Dubois, Thomas [Auteur]
MICrobiologie de l'ALImentation au Service de la Santé [MICALIS]
Lemy, Christelle [Auteur]
MICrobiologie de l'ALImentation au Service de la Santé [MICALIS]
Perchat, Stéphane [Auteur]
Lereclus, Didier [Auteur]
MICrobiologie de l'ALImentation au Service de la Santé [MICALIS]
Lemy, Christelle [Auteur]
MICrobiologie de l'ALImentation au Service de la Santé [MICALIS]
Perchat, Stéphane [Auteur]
Lereclus, Didier [Auteur]
Journal title :
Molecular Microbiology
Abbreviated title :
Mol Microbiol
Volume number :
112
Pages :
219-232
Publisher :
Wiley
Publication date :
2019-05-11
HAL domain(s) :
Sciences du Vivant [q-bio]/Ingénierie des aliments
English abstract : [en]
The infectious cycle of Bacillus thuringiensis in the insect host is regulated by quorum sensors of the RNPP family. The activity of these regulators is modulated by their cognate signaling peptides translocated into the ...
Show more >The infectious cycle of Bacillus thuringiensis in the insect host is regulated by quorum sensors of the RNPP family. The activity of these regulators is modulated by their cognate signaling peptides translocated into the bacterial cells by oligopeptide permeases (Opp systems). In B. thuringiensis, the quorum sensor NprR is a bi‐functional regulator that connects sporulation to necrotrophism. The binding of the signaling peptide NprX switches NprR from a dimeric inhibitor of sporulation to a tetrameric transcriptional activator involved in the necrotrophic lifestyle of B. thuringiensis. Here, we report that NprX is imported into the bacterial cells by two different oligopeptide permease systems. The first one is Opp, the system known to be involved in the import of the signaling peptide PapR in B. thuringiensis and Bacillus cereus. The second, designated as Npp (NprX peptide permease), was not previously described. We show that at least two substrate binding proteins (SBPs) are able to translocate NprX through OppBCDF. In contrast, we demonstrate that a unique SBP (NppA) can translocate NprX through NppDFBC. We identified the promoter of the npp operon, and we showed that transcription starts at the onset of stationary phase and is repressed by the nutritional regulator CodY during the exponential growth phase.Show less >
Show more >The infectious cycle of Bacillus thuringiensis in the insect host is regulated by quorum sensors of the RNPP family. The activity of these regulators is modulated by their cognate signaling peptides translocated into the bacterial cells by oligopeptide permeases (Opp systems). In B. thuringiensis, the quorum sensor NprR is a bi‐functional regulator that connects sporulation to necrotrophism. The binding of the signaling peptide NprX switches NprR from a dimeric inhibitor of sporulation to a tetrameric transcriptional activator involved in the necrotrophic lifestyle of B. thuringiensis. Here, we report that NprX is imported into the bacterial cells by two different oligopeptide permease systems. The first one is Opp, the system known to be involved in the import of the signaling peptide PapR in B. thuringiensis and Bacillus cereus. The second, designated as Npp (NprX peptide permease), was not previously described. We show that at least two substrate binding proteins (SBPs) are able to translocate NprX through OppBCDF. In contrast, we demonstrate that a unique SBP (NppA) can translocate NprX through NppDFBC. We identified the promoter of the npp operon, and we showed that transcription starts at the onset of stationary phase and is repressed by the nutritional regulator CodY during the exponential growth phase.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
CNRS
INRA
ENSCL
CNRS
INRA
ENSCL
Collections :
Research team(s) :
Processus aux Interfaces et Hygiène des Matériaux (PIHM)
Submission date :
2020-12-14T15:18:33Z