The structural organization of the N-terminus ...
Type de document :
Article dans une revue scientifique
PMID :
URL permanente :
Titre :
The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners
Auteur(s) :
Roblin, Pierre [Auteur]
Synchrotron SOLEIL [SSOLEIL]
Unité de recherche sur les Biopolymères, Interactions Assemblages [BIA]
Lebrun, Pierre [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Rucktooa, Prakash [Auteur]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Dewitte, Frederique [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Lens, Zoe [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Receveur-Brechot, Véronique [Auteur]
Centre de Recherche en Cancérologie de Marseille [CRCM]
Raussens, Vincent [Auteur]
Faculté des Sciences [Bruxelles] [ULB]
Villeret, Vincent [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Bompard, Coralie [Auteur]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Centre National de la Recherche Scientifique [CNRS]
Synchrotron SOLEIL [SSOLEIL]
Unité de recherche sur les Biopolymères, Interactions Assemblages [BIA]
Lebrun, Pierre [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Rucktooa, Prakash [Auteur]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Dewitte, Frederique [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Lens, Zoe [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Receveur-Brechot, Véronique [Auteur]
Centre de Recherche en Cancérologie de Marseille [CRCM]
Raussens, Vincent [Auteur]
Faculté des Sciences [Bruxelles] [ULB]
Villeret, Vincent [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Bompard, Coralie [Auteur]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Centre National de la Recherche Scientifique [CNRS]
Titre de la revue :
Biochimica et biophysica acta
Nom court de la revue :
Biochim. Biophys. Acta
Numéro :
1834
Pagination :
2564-2572
Date de publication :
2013-12
ISSN :
0006-3002
Mot(s)-clé(s) en anglais :
Sigma Factor
CBD
TTSS
circular dichroism
Salmonella typhimurium
Type three secretion system
Protein Structure, Quaternary
Chaperone binding domain
Salmonella outer protein B
R(g)
Protein Structure, Tertiary
DSP
CD
Molecular Chaperones
Protein Structure, Secondary
Bacterial virulence
radius of gyration
SopB
Bacterial Proteins
hydrodynamic radius
SAXS
R(h)
Intrinsically disordered protein
Small angle X-ray scattering
dithio-bis-(succinimidylpropionate)
CBD
TTSS
circular dichroism
Salmonella typhimurium
Type three secretion system
Protein Structure, Quaternary
Chaperone binding domain
Salmonella outer protein B
R(g)
Protein Structure, Tertiary
DSP
CD
Molecular Chaperones
Protein Structure, Secondary
Bacterial virulence
radius of gyration
SopB
Bacterial Proteins
hydrodynamic radius
SAXS
R(h)
Intrinsically disordered protein
Small angle X-ray scattering
dithio-bis-(succinimidylpropionate)
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
The TTSS is used by Salmonella and many bacterial pathogens to inject virulence factors directly into the cytoplasm of target eukaryotic cells. Once translocated these so-called effector proteins hijack a vast array of ...
Lire la suite >The TTSS is used by Salmonella and many bacterial pathogens to inject virulence factors directly into the cytoplasm of target eukaryotic cells. Once translocated these so-called effector proteins hijack a vast array of crucial cellular functions to the benefit of the bacteria. In the bacterial cytoplasm, some effectors are stabilized and maintained in a secretion competent state by interaction with specific type III chaperones. In this work we studied the conformation of the Chaperone Binding Domain of the effector named Salmonella Outer protein B (SopB) alone and in complex with its cognate chaperone SigE by a combination of biochemical, biophysical and structural approaches. Our results show that the N-terminus part of SopB is mainly composed by α-helices and unfolded regions whose organization/stabilization depends on their interaction with the different partners. This suggests that the partially unfolded state of this N-terminal region, which confers the adaptability of the effector to bind very different partners during the infection cycle, allows the bacteria to modulate numerous host cells functions limiting the number of translocated effectors.Lire moins >
Lire la suite >The TTSS is used by Salmonella and many bacterial pathogens to inject virulence factors directly into the cytoplasm of target eukaryotic cells. Once translocated these so-called effector proteins hijack a vast array of crucial cellular functions to the benefit of the bacteria. In the bacterial cytoplasm, some effectors are stabilized and maintained in a secretion competent state by interaction with specific type III chaperones. In this work we studied the conformation of the Chaperone Binding Domain of the effector named Salmonella Outer protein B (SopB) alone and in complex with its cognate chaperone SigE by a combination of biochemical, biophysical and structural approaches. Our results show that the N-terminus part of SopB is mainly composed by α-helices and unfolded regions whose organization/stabilization depends on their interaction with the different partners. This suggests that the partially unfolded state of this N-terminal region, which confers the adaptability of the effector to bind very different partners during the infection cycle, allows the bacteria to modulate numerous host cells functions limiting the number of translocated effectors.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Collections :
Équipe(s) de recherche :
Glycobiologie végétale
Biologie structurale et intégrative
Biologie structurale et intégrative
Date de dépôt :
2020-02-12T15:11:29Z
2021-03-11T14:34:33Z
2021-03-11T14:34:33Z