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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cordier, Baptiste Grangeasse, Christophe Freton, Céline Galinier, Anne Foulquier, Elodie Pompeo, Frédérique |
| Description | Author Affiliation: Foulquier E ( From the Laboratoire de Chimie Bactérienne, UMR 7283, Institut de Microbiologie de la Méditerranée, CNRS, Aix-Marseille Université, 13009 Marseille and.); Pompeo F ( From the Laboratoire de Chimie Bactérienne, UMR 7283, Institut de Microbiologie de la Méditerranée, CNRS, Aix-Marseille Université, 13009 Marseille and.); Freton C ( From the Laboratoire de Chimie Bactérienne, UMR 7283, Institut de Microbiologie de la Méditerranée, CNRS, Aix-Marseille Université, 13009 Marseille and the Bases Moléculaires et Structurales des Systèmes Infectieux, UMR 5086, CNRS, Université de Lyon, 69367 Lyon Cedex 07, France.); Cordier B ( From the Laboratoire de Chimie Bactérienne, UMR 7283, Institut de Microbiologie de la Méditerranée, CNRS, Aix-Marseille Université, 13009 Marseille and.); Grangeasse C ( the Bases Moléculaires et Structurales des Systèmes Infectieux, UMR 5086, CNRS, Université de Lyon, 69367 Lyon Cedex 07, France.); Galinier A ( From the Laboratoire de Chimie Bactérienne, UMR 7283, Institut de Microbiologie de la Méditerranée, CNRS, Aix-Marseille Université, 13009 Marseille and galinier@imm.cnrs.fr.) |
| Abstract | The YvcK protein has been shown to be necessary for growth under gluconeogenic conditions in Bacillus subtilis. Amazingly, its overproduction rescues growth and morphology defects of the actin-like protein MreB deletion mutant by restoration of PBP1 localization. In this work, we observed that YvcK was phosphorylated at Thr-304 by the protein kinase PrkC and that phosphorylated YvcK was dephosphorylated by the cognate phosphatase PrpC. We show that neither substitution of this threonine with a constitutively phosphorylated mimicking glutamic acid residue or a phosphorylation-dead mimicking alanine residue nor deletion of prkC or prpC altered the ability of B. subtilis to grow under gluconeogenic conditions. However, we observed that a prpC mutant and a yvcK mutant were more sensitive to bacitracin compared with the WT strain. In addition, the bacitracin sensitivity of strains in which YvcK Thr-304 was replaced with either an alanine or a glutamic acid residue was also affected. We also analyzed rescue of the mreB mutant strain by overproduction of YvcK in which the phosphorylation site was substituted. We show that YvcK T304A overproduction did not rescue the mreB mutant aberrant morphology due to PBP1 mislocalization. The same observation was made in an mreB prkC double mutant overproducing YvcK. Altogether, these data show that YvcK may have two distinct functions: 1) in carbon source utilization independent of its phosphorylation level and 2) in cell wall biosynthesis and morphogenesis through its phosphorylation state. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 34 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-08-22 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Bacillus Subtilis Metabolism Bacterial Proteins Physiology Mutation Amino Acid Sequence Drug Effects Genetics Bacitracin Pharmacology Chemistry Blotting, Western Drug Resistance, Bacterial Molecular Sequence Data Phosphorylation Tandem Mass Spectrometry Threonine Two-Hybrid System Techniques Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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