ArticleMolecular & cellular proteomics : MCP2018
N-terminal Acetylation Levels Are Maintained During Acetyl-CoA Deficiency in
Article in Molecular & cellular proteomics : MCP, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 30 citations in OpenAlex.
- Fine mapping and prediction of a candidate gene for wrinkled rind in melon (Cucumis melo L.).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025Article
- Mechanisms of metabolism-coupled protein modifications.Nature chemical biology · 2025Review
- N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity.Nature communications · 2023Article
- Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae.Nature communications · 2023Article
- Up-regulation of ubiquitin-proteasome activity upon loss of NatA-dependent N-terminal acetylation.Life science alliance · 2022Article
- Human NAA30 can rescue yeast mak3∆ mutant growth phenotypes.Bioscience reports · 2021Article
- Overlap of NatA and IAP substrates implicates N-terminal acetylation in protein stabilization.Science advances · 2021Article
- N-terminal protein acetylation by NatB modulates the levels of Nmnats, the NADThe Journal of biological chemistry · 2020Article
- Chromatin-sensitive cryptic promoters putatively drive expression of alternative protein isoforms in yeast.Genome research · 2019Article
- Article
- Ablation of elongation factor 2 kinase enhances heat-shock protein 90 chaperone expression and protects cells under proteotoxic stress.The Journal of biological chemistry · 2019Article
- Co-translational, Post-translational, and Non-catalytic Roles of N-Terminal Acetyltransferases.Molecular cell · 2019Review
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
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 (
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