Academic Journal
N-terminal acetylation levels are maintained during acetyl-CoA deficiency in Saccharomyces cerevisiae
| العنوان: | N-terminal acetylation levels are maintained during acetyl-CoA deficiency in Saccharomyces cerevisiae |
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| المؤلفون: | Varland, Sylvia, Aksnes, Henriette, Kryuchkov, Fedor, Impens, Francis, Van Haver, Delphi, Jonckheere, Veronique, Ziegler, Mathias, Gevaert, Kris, Van Damme, Petra, Arnesen, Thomas |
| المصدر: | MOLECULAR & CELLULAR PROTEOMICS ; ISSN: 1535-9476 ; ISSN: 1535-9484 |
| سنة النشر: | 2018 |
| المجموعة: | Ghent University Academic Bibliography |
| مصطلحات موضوعية: | Biology and Life Sciences, 60S RIBOSOMAL-SUBUNITS, CELLULAR-PROTEINS, ALPHA-ACETYLATION, HISTONE ACETYLATION, GTPASE ARL3P, IN-VIVO, YEAST, ACETYLTRANSFERASE, METABOLISM, REVEALS |
| الوصف: | N-terminal acetylation (Nt-acetylation) is a highly abundant protein modification in eukaryotes and impacts a wide range of cellular processes, including protein quality control and stress tolerance. Despite its prevalence, the mechanisms regulating Nt-acetylation are still nebulous. Here, we present the first global study of Nt-acetylation in yeast cells as they progress to stationary phase in response to nutrient starvation. Surprisingly, we found that yeast cells maintain their global Nt-acetylation levels upon nutrient depletion, despite a marked decrease in acetyl-CoA levels. We further observed two distinct sets of protein N termini that display differential and opposing Nt-acetylation behavior upon nutrient starvation, indicating a dynamic process. The first protein cluster was enriched for annotated N termini showing increased Nt-acetylation in stationary phase compared with exponential growth phase. The second protein cluster was conversely enriched for alternative nonannotated N termini (i.e. N termini indicative of shorter N-terminal proteoforms) and, like histones, showed reduced acetylation levels in stationary phase when acetyl-CoA levels were low. Notably, the degree of Nt-acetylation of Pcl8, a negative regulator of glycogen biosynthesis and two components of the pre-ribosome complex (Rsa3 and Rpl7a) increased during starvation. Moreover, the steady-state levels of these proteins were regulated both by starvation and NatA activity. In summary, this study represents the first comprehensive analysis of metabolic regulation of Nt-acetylation and reveals that specific, rather than global, Nt-acetylation events are subject to metabolic regulation. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| Relation: | https://biblio.ugent.be/publication/8581652; http://hdl.handle.net/1854/LU-8581652; http://dx.doi.org/10.1074/mcp.ra118.000982; https://biblio.ugent.be/publication/8581652/file/8581654 |
| DOI: | 10.1074/mcp.ra118.000982 |
| الاتاحة: | https://biblio.ugent.be/publication/8581652 http://hdl.handle.net/1854/LU-8581652 https://doi.org/10.1074/mcp.ra118.000982 https://biblio.ugent.be/publication/8581652/file/8581654 |
| Rights: | No license (in copyright) ; info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.2C7C4A8B |
| قاعدة البيانات: | BASE |
| DOI: | 10.1074/mcp.ra118.000982 |
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