The DivJ, CbrA and PleC system controls ...
Type de document :
Article dans une revue scientifique
DOI :
PMID :
URL permanente :
Titre :
The DivJ, CbrA and PleC system controls DivK phosphorylation and symbiosis in Sinorhizobium meliloti
Auteur(s) :
Pini, Francesco [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Frage, Benjamin [Auteur]
LOEWE Center for Synthetic Microbiology [SYNMIKRO]
Ferri, Lorenzo [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
De Nisco, Nicole J. [Auteur]
Massachusetts Institute of Technology [MIT]
Mohapatra, Saswat S. [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Taddei, Lucilla [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Fioravanti, Antonella [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Dewitte, Frederique [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Galardini, Marco [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Brilli, Matteo [Auteur]
Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 [LBBE]
Villeret, Vincent [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Bazzicalupo, Marco [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Mengoni, Alessio [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Walker, Graham C. [Auteur]
Massachusetts Institute of Technology [MIT]
Becker, Anke [Auteur]
LOEWE Center for Synthetic Microbiology [SYNMIKRO]
Biondi, Emanuele G. [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Centre National de la Recherche Scientifique [CNRS]
Frage, Benjamin [Auteur]
LOEWE Center for Synthetic Microbiology [SYNMIKRO]
Ferri, Lorenzo [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
De Nisco, Nicole J. [Auteur]
Massachusetts Institute of Technology [MIT]
Mohapatra, Saswat S. [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Taddei, Lucilla [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Fioravanti, Antonella [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Dewitte, Frederique [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Galardini, Marco [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Brilli, Matteo [Auteur]
Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 [LBBE]
Villeret, Vincent [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Bazzicalupo, Marco [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Mengoni, Alessio [Auteur]
Università degli Studi di Firenze = University of Florence = Université de Florence [UniFI]
Walker, Graham C. [Auteur]
Massachusetts Institute of Technology [MIT]
Becker, Anke [Auteur]
LOEWE Center for Synthetic Microbiology [SYNMIKRO]
Biondi, Emanuele G. [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Titre de la revue :
Molecular Microbiology
Nom court de la revue :
Mol. Microbiol.
Numéro :
90
Pagination :
54-71
Date de publication :
2013-10
ISSN :
1365-2958
Mot(s)-clé(s) en anglais :
Symbiosis
Phosphorylation
Medicago sativa
Protein Processing, Post-Translational
Gene Expression Regulation, Bacterial
Sinorhizobium meliloti
Bacterial Proteins
Phosphorylation
Medicago sativa
Protein Processing, Post-Translational
Gene Expression Regulation, Bacterial
Sinorhizobium meliloti
Bacterial Proteins
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
Sinorhizobium meliloti is a soil bacterium that invades the root nodules it induces on Medicago sativa, whereupon it undergoes an alteration of its cell cycle and differentiates into nitrogen-fixing, elongated and polyploid ...
Lire la suite >Sinorhizobium meliloti is a soil bacterium that invades the root nodules it induces on Medicago sativa, whereupon it undergoes an alteration of its cell cycle and differentiates into nitrogen-fixing, elongated and polyploid bacteroid with higher membrane permeability. In Caulobacter crescentus, a related alphaproteobacterium, the principal cell cycle regulator, CtrA, is inhibited by the phosphorylated response regulator DivK. The phosphorylation of DivK depends on the histidine kinase DivJ, while PleC is the principal phosphatase for DivK. Despite the importance of the DivJ in C. crescentus, the mechanistic role of this kinase has never been elucidated in other Alphaproteobacteria. We show here that the histidine kinases DivJ together with CbrA and PleC participate in a complex phosphorylation system of the essential response regulator DivK in S. meliloti. In particular, DivJ and CbrA are involved in DivK phosphorylation and in turn CtrA inactivation, thereby controlling correct cell cycle progression and the integrity of the cell envelope. In contrast, the essential PleC presumably acts as a phosphatase of DivK. Interestingly, we found that a DivJ mutant is able to elicit nodules and enter plant cells, but fails to establish an effective symbiosis suggesting that proper envelope and/or low CtrA levels are required for symbiosis.Lire moins >
Lire la suite >Sinorhizobium meliloti is a soil bacterium that invades the root nodules it induces on Medicago sativa, whereupon it undergoes an alteration of its cell cycle and differentiates into nitrogen-fixing, elongated and polyploid bacteroid with higher membrane permeability. In Caulobacter crescentus, a related alphaproteobacterium, the principal cell cycle regulator, CtrA, is inhibited by the phosphorylated response regulator DivK. The phosphorylation of DivK depends on the histidine kinase DivJ, while PleC is the principal phosphatase for DivK. Despite the importance of the DivJ in C. crescentus, the mechanistic role of this kinase has never been elucidated in other Alphaproteobacteria. We show here that the histidine kinases DivJ together with CbrA and PleC participate in a complex phosphorylation system of the essential response regulator DivK in S. meliloti. In particular, DivJ and CbrA are involved in DivK phosphorylation and in turn CtrA inactivation, thereby controlling correct cell cycle progression and the integrity of the cell envelope. In contrast, the essential PleC presumably acts as a phosphatase of DivK. Interestingly, we found that a DivJ mutant is able to elicit nodules and enter plant cells, but fails to establish an effective symbiosis suggesting that proper envelope and/or low CtrA levels are required for symbiosis.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Collections :
Équipe(s) de recherche :
Biologie structurale et intégrative
Date de dépôt :
2020-02-12T15:11:30Z
2021-03-11T14:21:11Z
2021-03-11T14:21:11Z