CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis
| Autor: | Edwige Madec, Simone J. Séror, Delphine Delattre, I. Barry Holland, Michał Obuchowski, Cédric Absalon |
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| Přispěvatelé: | Institut de génétique et microbiologie [Orsay] (IGM), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Threonine
Phosphatase GTPase Bacillus subtilis Biology Peptide Elongation Factor Tu Protein Serine-Threonine Kinases Microbiology MESH: Protein-Serine-Threonine Kinases Substrate Specificity Serine 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins MESH: Peptide Elongation Factor Tu MESH: Phosphoprotein Phosphatases Escherichia coli Phosphoprotein Phosphatases [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Translation factor MESH: Serine Phosphorylation MESH: Threonine MESH: Bacterial Proteins 030304 developmental biology 0303 health sciences MESH: Phosphorylation 030306 microbiology Kinase MESH: Escherichia coli MESH: Bacillus subtilis biology.organism_classification PASTA domain MESH: Mutagenesis Site-Directed [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology chemistry Biochemistry Mutagenesis Site-Directed MESH: Substrate Specificity Peptidoglycan |
| Zdroj: | Microbiology Microbiology, Microbiology Society, 2009, 155 (Pt 3), pp.932-43. ⟨10.1099/mic.0.022475-0⟩ |
| ISSN: | 1350-0872 1465-2080 |
| DOI: | 10.1099/mic.0.022475-0⟩ |
| Popis: | The conservedprpC,prkC,cpgAlocus inBacillus subtilisencodes respectively a Ser/Thr phosphatase, the cognate sensor kinase (containing an external PASTA domain suggested to bind peptidoglycan precursors) and CpgA, a small ribosome-associated GTPase that we have shown previously is implicated in shape determination and peptidoglycan deposition. In this study, in a search for targets of PrkC and PrpC, we showed that,in vitro, CpgA itself is phosphorylated on serine and threonine, and another GTPase, the translation factor EF-Tu, is also phosphorylated by the kinase on the conserved T384 residue. Both substrates are dephosphorylated by PrpCin vitro. In addition, we identified YezB, a 10.3 kDa polypeptide, and a component of the stressosome, as a substrate for both enzymesin vitroand apparentlyin vivo. We propose that the PrpC/PrkC/CpgA system constitutes an important element of a regulatory network involved in the coordination of cell wall expansion and growth inB. subtilis. |
| Databáze: | OpenAIRE |
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