The DivJ, CbrA and PleC system controls ...
Document type :
Article dans une revue scientifique
DOI :
PMID :
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Title :
The DivJ, CbrA and PleC system controls DivK phosphorylation and symbiosis in Sinorhizobium meliloti
Author(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]
Journal title :
Molecular Microbiology
Abbreviated title :
Mol. Microbiol.
Volume number :
90
Pages :
54-71
Publication date :
2013-10
ISSN :
1365-2958
English keyword(s) :
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
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [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 ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Collections :
Research team(s) :
Biologie structurale et intégrative
Submission date :
2020-02-12T15:11:30Z
2021-03-11T14:21:11Z
2021-03-11T14:21:11Z