Interaction of GapA with HPr and Its Homologue, Crh: Novel Levels of Regulation of a Key Step of Glycolysis in Bacillus subtilis?▿ †
| Autor: | Anne Galinier, Frédérique Pompeo, Jennifer Luciano |
|---|---|
| Přispěvatelé: | 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) |
| Jazyk: | angličtina |
| Rok vydání: | 2006 |
| Předmět: |
Blotting
Western Dehydrogenase Genetics and Molecular Biology Plasma protein binding Bacillus subtilis macromolecular substances Protein Serine-Threonine Kinases Microbiology Chromatography Affinity 03 medical and health sciences Bacterial Proteins Glycolysis Molecular Biology ComputingMilieux_MISCELLANEOUS Glyceraldehyde 3-phosphate dehydrogenase 030304 developmental biology chemistry.chemical_classification 0303 health sciences Bacillaceae biology 030306 microbiology Glyceraldehyde-3-Phosphate Dehydrogenases Gene Expression Regulation Bacterial biology.organism_classification 3. Good health carbohydrates (lipids) [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology Enzyme Spectrometry Fluorescence Biochemistry chemistry biology.protein Phosphorylation bacteria Electrophoresis Polyacrylamide Gel Protein Binding |
| Zdroj: | Journal of Bacteriology Journal of Bacteriology, American Society for Microbiology, 2007, 189 (3), pp.1154-1157. ⟨10.1128/JB.01575-06⟩ |
| ISSN: | 0021-9193 1098-5530 |
| DOI: | 10.1128/JB.01575-06⟩ |
| Popis: | In Bacillus subtilis cells, we identified a new partner of HPr, an enzyme of the glycolysis pathway, the glyceraldehyde-3-phosphate dehydrogenase GapA. We showed that, in vitro, phosphorylated and unphosphorylated forms of HPr and its homologue, Crh, could interact with GapA, but only their seryl-phosphorylated forms were able to inhibit its activity. |
| Databáze: | OpenAIRE |
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