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N-terminal acetylation levels are maintained during acetyl-CoA deficiency in Saccharomyces cerevisiae

(2018) MOLECULAR & CELLULAR PROTEOMICS. 17(12). p.2308-2323
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Abstract
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.
Keywords
60S RIBOSOMAL-SUBUNITS, CELLULAR-PROTEINS, ALPHA-ACETYLATION, HISTONE ACETYLATION, GTPASE ARL3P, IN-VIVO, YEAST, ACETYLTRANSFERASE, METABOLISM, REVEALS

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Chicago
Varland, Sylvia, Henriette Aksnes, Fedor Kryuchkov, Francis Impens, Delphi Van Haver, Veronique Jonckheere, Mathias Ziegler, Kris Gevaert, Petra Van Damme, and Thomas Arnesen. 2018. “N-terminal Acetylation Levels Are Maintained During acetyl-CoA Deficiency in Saccharomyces Cerevisiae.” Molecular & Cellular Proteomics 17 (12): 2308–2323.
APA
Varland, S., Aksnes, H., Kryuchkov, F., Impens, F., Van Haver, D., Jonckheere, V., Ziegler, M., et al. (2018). N-terminal acetylation levels are maintained during acetyl-CoA deficiency in Saccharomyces cerevisiae. MOLECULAR & CELLULAR PROTEOMICS, 17(12), 2308–2323.
Vancouver
1.
Varland S, Aksnes H, Kryuchkov F, Impens F, Van Haver D, Jonckheere V, et al. N-terminal acetylation levels are maintained during acetyl-CoA deficiency in Saccharomyces cerevisiae. MOLECULAR & CELLULAR PROTEOMICS. 2018;17(12):2308–23.
MLA
Varland, Sylvia, Henriette Aksnes, Fedor Kryuchkov, et al. “N-terminal Acetylation Levels Are Maintained During acetyl-CoA Deficiency in Saccharomyces Cerevisiae.” MOLECULAR & CELLULAR PROTEOMICS 17.12 (2018): 2308–2323. Print.
@article{8581652,
  abstract     = {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.},
  author       = {Varland, Sylvia and Aksnes, Henriette and Kryuchkov, Fedor and Impens, Francis and Van Haver, Delphi and Jonckheere, Veronique and Ziegler, Mathias and Gevaert, Kris and Van Damme, Petra and Arnesen, Thomas},
  issn         = {1535-9476},
  journal      = {MOLECULAR \& CELLULAR PROTEOMICS},
  language     = {eng},
  number       = {12},
  pages        = {2308--2323},
  title        = {N-terminal acetylation levels are maintained during acetyl-CoA deficiency in Saccharomyces cerevisiae},
  url          = {http://dx.doi.org/10.1074/mcp.ra118.000982},
  volume       = {17},
  year         = {2018},
}

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