ArticleNature communications2023
Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- The ribosome-associated N-terminal acetyltransferase B coordinates global proteostasis and autophagy in plants by creating Ac/N-degrons.Nature communications · 2026Article
- SIRT1-mediated FABP4 destabilization attenuates fibrosis and ferroptosis in non-alcoholic fatty liver disease.Clinical and experimental medicine · 2026Article
- Ribosomal expansion segment contributes to translation fidelity via N-terminal processing of ribosomal proteins.Nucleic acids research · 2025Article
- Ribosome-associated proteins: unwRAPping ribosome heterogeneity in the twenty-first century.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- Illuminating the impact of N-terminal acetylation: from protein to physiology.Nature communications · 2025Review
- Guided tour through the small protein landscape ofmicroLife · 2025Article
- Characterizing protein-protein interactions with thermal proteome profiling.Current opinion in structural biology · 2024Review
- Conformational plasticity links structural instability of NAA10Computational and structural biotechnology journal · 2024Article
- The lowdown on breakdown: Open questions in plant proteolysis.The Plant cell · 2024Review
- Automated Immunoprecipitation Workflow for Comprehensive Acetylome Analysis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Acetyltransferase in cardiovascular disease and aging.The journal of cardiovascular aging · 2024Article
- N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity.Nature communications · 2023Article
- Article
- N-terminal acetylation can stabilize proteins independent of their ubiquitination.Scientific reports · 2023Article
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Protein N-terminal (Nt) acetylation is one of the most abundant modifications in eukaryotes, covering ~50-80 % of the proteome, depending on species. Cells with defective Nt-acetylation display a wide array of phenotypes such as impaired growth, mating defects and increased stress sensitivity. However, the pleiotropic nature of these effects has hampered our understanding of the functional impact of protein Nt-acetylation. The main enzyme responsible for Nt-acetylation throughout the eukaryotic kingdom is the N-terminal acetyltransferase NatA. Here we employ a multi-dimensional proteomics approach to analyze Saccharomyces cerevisiae lacking NatA activity, which causes global proteome remodeling. Pulsed-SILAC experiments reveals that NatA-deficient strains consistently increase degradation of ribosomal proteins compared to wild type. Explaining this phenomenon, thermal proteome profiling uncovers decreased thermostability of ribosomes in NatA-knockouts. Our data are in agreement with a role for Nt-acetylation in promoting stability for parts of the proteome by enhancing the avidity of protein-protein interactions and folding.
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