N-terminal Acetylation Levels Are Maintained During Acetyl-CoA Deficiency in Saccharomyces cerevisiae.

Molecular & Cellular Proteomics : MCP
Sylvia VarlandThomas Arnesen

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 regulato...Continue Reading

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Datasets Mentioned

BETA
PXD004326
PXD009214

Methods Mentioned

BETA
acetylation
protein folding
environmental stress
histone acetylation
PCR
acetylate

Software Mentioned

Viewer
GO Slim Mapper
Perseus
MaxQuant
MS
SIEVE
Andromeda
Mascot Distiller Quantitation Tool
ImageLab
Mascot

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