Serine/threonine protein kinase PrkA of the human pathogen Listeriamonocytogenes: Biochemical characterization and identification of interacting partners through proteomic approaches
Listeria monocytogenes is the causative agent of listeriosis, a very serious food-borne human disease. The analysis of the proteins coded by the L. monocytogenes genome reveals the presence of two eukaryotic-type Ser/Thr-kinases (lmo1820 and lmo0618) and a Ser/Thrphosphatase (lmo1821). Protein phosp...
| Autores: | ; ; ; ; ; ; ; ; |
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| Tipo de documento: | Artículo |
| Estado: | Published version |
| Fecha de publicación: | 2011 |
| País: | Uruguay |
| Institución: | Institut Pasteur de Montevideo |
| Repositorio: | IPMON en REDI |
| Lenguaje: | Inglés |
| OAI Identifier: | oai:redi.anii.org.uy:20.500.12381/186 |
| Acceso en línea: | http://hdl.handle.net/20.500.12381/186 https://doi.org/10.1016/j.jprot.2011.03.005 |
| Nivel de acceso: | Acceso abierto |
| Palabra clave: | PknG Serine/Threonine protein kinase Glutamine synthetase FhaA Affinity Purification-mass spectrometry Mycobacterium tuberculosis Ciencias Naturales y Exactas Ciencias Biológicas Bioquímica y Biología Molecular |
| Sumario: | Listeria monocytogenes is the causative agent of listeriosis, a very serious food-borne human disease. The analysis of the proteins coded by the L. monocytogenes genome reveals the presence of two eukaryotic-type Ser/Thr-kinases (lmo1820 and lmo0618) and a Ser/Thrphosphatase (lmo1821). Protein phosphorylation regulates enzyme activities and protein interactions participating in physiological and pathophysiological processes in bacterial diseases. However in the case of L. monocytogenes there is scarce information about biochemical properties of these enzymes, as well as the physiological processes that they modulate. In the present work the catalytic domain of the protein coded by lmo1820 was produced as a functional His6-tagged Ser/Thr-kinase, and was denominated PrkA. PrkA was able to autophosphorylate specific Thr residues within its activation loop sequence. A similar autophosphorylation pattern was previously reported for Ser/Thr-kinases from related prokaryotes, whose role in kinase activity and substrate recruitment was demonstrated. We studied the kinase interactome using affinity chromatography and proteomic approaches. We identified 62 proteins that interact, either directly or indirectly, with the catalytic domain of PrkA, including proteins that participate in carbohydrates metabolism, cell wall metabolism and protein synthesis. Our results suggest that PrkA could be involved in the regulation of a variety of fundamental biological processes. |
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