The expanded specificity and physiological role of a widespread N-degron recognin
العنوان: | The expanded specificity and physiological role of a widespread N-degron recognin |
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المؤلفون: | Jinki Yeom, Eduardo A. Groisman, Xiaohui Gao |
المصدر: | Proceedings of the National Academy of Sciences. 116:18629-18637 |
بيانات النشر: | Proceedings of the National Academy of Sciences, 2019. |
سنة النشر: | 2019 |
مصطلحات موضوعية: | Proteases, medicine.medical_treatment, Proteolysis, Guanosine Tetraphosphate, Substrate Specificity, 03 medical and health sciences, chemistry.chemical_compound, Bacterial Proteins, medicine, Amino Acids, Pyrophosphatases, Tyrosine, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Multidisciplinary, Protease, Methionine, medicine.diagnostic_test, 030306 microbiology, Salmonella enterica, Amino acid, PNAS Plus, Biochemistry, chemistry, Degron, Carrier Proteins, Hydrophobic and Hydrophilic Interactions, Peptide Hydrolases, Protein Binding, Alarmone |
الوصف: | All cells use proteases to maintain protein homeostasis. The proteolytic systems known as the N-degron pathways recognize signals at the N terminus of proteins and bring about the degradation of these proteins. The ClpS protein enforces the N-degron pathway in bacteria and bacteria-derived organelles by targeting proteins harboring leucine, phenylalanine, tryptophan, or tyrosine at the N terminus for degradation by the protease ClpAP. We now report that ClpS binds, and ClpSAP degrades, proteins still harboring the N-terminal methionine. We determine that ClpS recognizes a type of degron in intact proteins based on the identity of the fourth amino acid from the N terminus, showing a strong preference for large hydrophobic amino acids. We uncover natural ClpS substrates in the bacterium Salmonella enterica, including SpoT, the essential synthase/hydrolase of the alarmone (p)ppGpp. Our findings expand both the specificity and physiological role of the widespread N-degron recognin ClpS. |
تدمد: | 1091-6490 0027-8424 |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e15547a880e7bd079741ecd562c1ca0 https://doi.org/10.1073/pnas.1821060116 |
حقوق: | OPEN |
رقم الأكسشن: | edsair.doi.dedup.....3e15547a880e7bd079741ecd562c1ca0 |
قاعدة البيانات: | OpenAIRE |
تدمد: | 10916490 00278424 |
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