Activator of one protease transforms into inhibitor of another in response to nutritional signals
| العنوان: | Activator of one protease transforms into inhibitor of another in response to nutritional signals |
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| المؤلفون: | Jinki Yeom, Eduardo A. Groisman |
| المصدر: | Genes & Development. 33:1280-1292 |
| بيانات النشر: | Cold Spring Harbor Laboratory, 2019. |
| سنة النشر: | 2019 |
| مصطلحات موضوعية: | Proteases, Protease La, medicine.medical_treatment, Proteolysis, Enzyme Activators, Biology, Substrate Specificity, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Bacterial Proteins, Genetics, medicine, Nutritional Physiological Phenomena, Enzyme Inhibitors, Heat-Shock Proteins, 030304 developmental biology, 0303 health sciences, Protease, medicine.diagnostic_test, Activator (genetics), Acetyl-CoA, Salmonella enterica, Acetylation, Metabolism, Cell biology, Glucose, chemistry, 030220 oncology & carcinogenesis, Proteome, Protein Binding, Research Paper, Developmental Biology |
| الوصف: | All cells use proteases to adjust protein amounts. Proteases maintain protein homeostasis by degrading nonfunctional toxic proteins and play regulatory roles by targeting particular substrates in response to specific signals. Here we address how cells tune protease specificity to nutritional signals. We report that Salmonella enterica increases the specificity of the broadly conserved proteases Lon and ClpSAP by transforming the Lon activator and substrate HspQ into an inhibitor of the N-degron recognin ClpS, the adaptor of the ClpAP protease. We establish that upon acetylation, HspQ stops being a Lon activator and substrate and that the accumulated HspQ binds to ClpS, hindering degradation of ClpSAP substrates. Growth on glucose promotes HspQ acetylation by increasing acetyl-CoA amounts, thereby linking metabolism to proteolysis. By altering protease specificities but continuing to degrade junk proteins, cells modify the abundance of particular proteins while preserving the quality of their proteomes. This rapid response mechanism linking protease specificity to nutritional signals is broadly conserved. |
| تدمد: | 1549-5477 0890-9369 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c9a959ec0e3d194e8b4c4873c96b3cb https://doi.org/10.1101/gad.325241.119 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....5c9a959ec0e3d194e8b4c4873c96b3cb |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15495477 08909369 |
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