From the Characterization of the Four Serine/Threonine Protein Kinases (PknA/B/G/L) of Corynebacterium glutamicum toward the Role of PknA and PknB in Cell Division
| Autor: | Marc J. Canova, Isabelle Zanella-Cléon, José A. Gil, Alain J. Cozzone, Michel Becchi, Luis M. Mateos, Virginie Molle, María Fiuza, Laurent Kremer |
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| Přispěvatelé: | Universidad de León [León], Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Dynamique des interactions membranaires normales et pathologiques (DIMNP), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Montpellier 1 (UM1) |
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Cell division
Molecular Sequence Data Mutant Serine threonine protein kinase Protein Serine-Threonine Kinases Biology Cell morphology Models Biological Biochemistry Corynebacterium glutamicum Phosphorylation cascade 03 medical and health sciences [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence Cloning Molecular Phosphorylation Molecular Biology 030304 developmental biology 0303 health sciences Binding Sites Models Genetic Sequence Homology Amino Acid 030306 microbiology Kinase Chemistry Gene Expression Regulation Bacterial Cell Biology Recombinant Proteins Mutation Additions and Corrections Cell Division Signal Transduction |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2008, 283 (26), pp.18099-112. ⟨10.1074/jbc.M802615200⟩ |
| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.M802615200⟩ |
| Popis: | Corynebacterium glutamicum contains four serine/threonine protein kinases (STPKs) named PknA, PknB, PknG, and PknL. Here we present the first biochemical and comparative analysis of all four C. glutamicum STPKs and investigate their potential role in cell shape control and peptidoglycan synthesis during cell division. In vitro assays demonstrated that, except for PknG, all STPKs exhibited autokinase activity. We provide evidence that activation of PknG is part of a phosphorylation cascade mechanism that relies on PknA activity. Following phosphorylation by PknA, PknG could transphosphorylate its specific substrate OdhI in vitro. A mass spectrometry profiling approach was also used to identify the phosphoresidues in all four STPKs. The results indicate that the nature, number, and localization of the phosphoacceptors varies from one kinase to the other. Disruption of either pknL or pknG in C. glutamicum resulted in viable mutants presenting a typical cell morphology and growth rate. In contrast, we failed to obtain null mutants of pknA or pknB, supporting the notion that these genes are essential. Conditional mutants of pknA or pknB were therefore created, leading to partial depletion of PknA or PknB. This resulted in elongated cells, indicative of a cell division defect. Moreover, overexpression of PknA or PknB in C. glutamicum resulted in a lack of apical growth and therefore a coccoid-like morphology. These findings indicate that pknA and pknB are key players in signal transduction pathways for the regulation of the cell shape and both are essential for sustaining corynebacterial growth. |
| Databáze: | OpenAIRE |
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