Titre :

The signaling peptide NprX controlling sporulation and necrotrophism is imported intoBacillus thuringiensisby two oligopeptide permease systems

Auteur(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]

Titre de la revue :

Molecular Microbiology

Nom court de la revue :

Mol Microbiol

Numéro :

112

Pagination :

219-232

Éditeur :

Wiley

Date de publication :

2019-05-11

Discipline(s) HAL :

Sciences du Vivant [q-bio]/Ingénierie des aliments

Résumé en anglais : [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 ...
Lire la suite >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.Lire moins >

Langue :

Anglais

Comité de lecture :

Oui

Audience :

Internationale

Vulgarisation :

Non

Établissement(s) :

Université de Lille
CNRS
INRA
ENSCL

Collections :

• Unité Matériaux et Transformations (UMET) - UMR 8207

Équipe(s) de recherche :

Processus aux Interfaces et Hygiène des Matériaux (PIHM)

Date de dépôt :

2020-12-14T15:18:33Z