A Salmonella type three secretion ...
Type de document :
Article dans une revue scientifique
DOI :
PMID :
URL permanente :
Titre :
A Salmonella type three secretion effector/chaperone complex adopts a hexameric ring-like structure
Auteur(s) :
Roblin, Pierre [Auteur]
Synchrotron SOLEIL [SSOLEIL]
Unité de recherche sur les Biopolymères, Interactions Assemblages [BIA]
Dewitte, Frederique [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Villeret, Vincent [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Biondi, Emanuele G. [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Bompard, Coralie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Synchrotron SOLEIL [SSOLEIL]
Unité de recherche sur les Biopolymères, Interactions Assemblages [BIA]
Dewitte, Frederique [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Villeret, Vincent [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Biondi, Emanuele G. [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Bompard, Coralie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Titre de la revue :
Journal of Bacteriology
Nom court de la revue :
J. Bacteriol.
Numéro :
197
Pagination :
688-698
Date de publication :
2015-02-15
ISSN :
1098-5530
Mot(s)-clé(s) en anglais :
Protein Structure, Tertiary
Molecular Chaperones
Sigma Factor
Bacterial Secretion Systems
Models, Molecular
Scattering, Small Angle
Salmonella typhimurium
Bacterial Proteins
Molecular Chaperones
Sigma Factor
Bacterial Secretion Systems
Models, Molecular
Scattering, Small Angle
Salmonella typhimurium
Bacterial Proteins
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
Many bacterial pathogens use type three secretion systems (T3SS) to inject virulence factors, named effectors, directly into the cytoplasm of target eukaryotic cells. Most of the T3SS components are conserved among plant ...
Lire la suite >Many bacterial pathogens use type three secretion systems (T3SS) to inject virulence factors, named effectors, directly into the cytoplasm of target eukaryotic cells. Most of the T3SS components are conserved among plant and animal pathogens, suggesting a common mechanism of recognition and secretion of effectors. However, no common motif has yet been identified for effectors allowing T3SS recognition. In this work, we performed a biochemical and structural characterization of the Salmonella SopB/SigE chaperone/effector complex by small-angle X-ray scattering (SAXS). Our results showed that the SopB/SigE complex is assembled in dynamic homohexameric-ring-shaped structures with an internal tunnel. In this ring, the chaperone maintains a disordered N-terminal end of SopB molecules, in a good position to be reached and processed by the T3SS. This ring dimensionally fits the ring-organized molecules of the injectisome, including ATPase hexameric rings; this organization suggests that this structural feature is important for ATPase recognition by T3SS. Our work constitutes the first evidence of the oligomerization of an effector, analogous to the organization of the secretion machinery, obtained in solution. As effectors share neither sequence nor structural identity, the quaternary oligomeric structure could constitute a strategy evolved to promote the specificity and efficiency of T3SS recognition.Lire moins >
Lire la suite >Many bacterial pathogens use type three secretion systems (T3SS) to inject virulence factors, named effectors, directly into the cytoplasm of target eukaryotic cells. Most of the T3SS components are conserved among plant and animal pathogens, suggesting a common mechanism of recognition and secretion of effectors. However, no common motif has yet been identified for effectors allowing T3SS recognition. In this work, we performed a biochemical and structural characterization of the Salmonella SopB/SigE chaperone/effector complex by small-angle X-ray scattering (SAXS). Our results showed that the SopB/SigE complex is assembled in dynamic homohexameric-ring-shaped structures with an internal tunnel. In this ring, the chaperone maintains a disordered N-terminal end of SopB molecules, in a good position to be reached and processed by the T3SS. This ring dimensionally fits the ring-organized molecules of the injectisome, including ATPase hexameric rings; this organization suggests that this structural feature is important for ATPase recognition by T3SS. Our work constitutes the first evidence of the oligomerization of an effector, analogous to the organization of the secretion machinery, obtained in solution. As effectors share neither sequence nor structural identity, the quaternary oligomeric structure could constitute a strategy evolved to promote the specificity and efficiency of T3SS recognition.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
Plant Storage Polysaccharides
Biologie structurale et intégrative
Biologie structurale et intégrative
Date de dépôt :
2020-02-12T15:11:27Z
2021-03-11T15:08:36Z
2021-03-11T15:08:36Z