ArticleBMC genomics2010
Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels.
Article in BMC genomics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 88 citations in OpenAlex.
- Crosstalk between protein kinases Pho85-Pho80 and Rim11 regulates Pah1 phosphatidate phosphatase function in lipid synthesis.The Journal of biological chemistry · 2026Article
- Molecular mechanisms of transhydrogenase activity and allosteric regulation in eukaryotic type II PHGDH Ser33.Nature communications · 2026Article
- Growth phase diets diminish histone acetyltransferase Gcn5 function and shorten lifespan of Drosophila males.EMBO reports · 2025Article
- Pex30-dependent membrane contact sites maintain ER lipid homeostasis.The Journal of cell biology · 2025Article
- Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024Review
- Sequential CRISPR screening reveals partial NatB inhibition as a strategy to mitigate alpha-synuclein levels in human neurons.Science advances · 2024Article
- Metabolic regulation of proteome stability via N-terminal acetylation controls male germline stem cell differentiation and reproduction.Nature communications · 2023Article
- In-Depth Characterization of Apoptosis N-Terminome Reveals a Link Between Caspase-3 Cleavage and Posttranslational N-Terminal Acetylation.Molecular & cellular proteomics : MCP · 2023Review
- Article
- The second intracellular loop of the yeast Trk1 potassium transporter is involved in regulation of activity, and interaction with 14-3-3 proteins.Computational and structural biotechnology journal · 2023Article
- Phosphorylation-mediated regulation of the Nem1-Spo7/Pah1 phosphatase cascade in yeast lipid synthesis.Advances in biological regulation · 2022Review
- Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.Nature communications · 2021Article
- Pex30-like proteins function as adaptors at distinct ER membrane contact sites.The Journal of cell biology · 2021Article
- Ready, SET, Go: Post-translational regulation of the histone lysine methylation network in budding yeast.The Journal of biological chemistry · 2021Review
- Structural basis of Naa20 activity towards a canonical NatB substrate.Communications biology · 2021Article
- Overlap of NatA and IAP substrates implicates N-terminal acetylation in protein stabilization.Science advances · 2021Article
- The Spo7 sequence LLI is required for Nem1-Spo7/Pah1 phosphatase cascade function in yeast lipid metabolism.The Journal of biological chemistry · 2020Article
- NatB-Mediated N-Terminal Acetylation Affects Growth and Biotic Stress Responses.Plant physiology · 2020Article
- Yck1 casein kinase I regulates the activity and phosphorylation of Pah1 phosphatidate phosphatase fromThe Journal of biological chemistry · 2019Article
- Protein kinase C mediates the phosphorylation of the Nem1-Spo7 protein phosphatase complex in yeast.The Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe addition of an acetyl group to protein N-termini is a widespread co-translational modification. NatB is one of the main N-acetyltransferases that targets a subset of proteins possessing an N-terminal methionine, but so far only a handful of substrates have been reported. Using a yeast nat3Δ strain, deficient for the catalytic subunit of NatB, we employed a quantitative proteomics strategy to identify NatB substrates and to characterize downstream effects in nat3Δ.
resultsComparing by proteomics WT and nat3Δ strains, using metabolic 15N isotope labeling, we confidently identified 59 NatB substrates, out of a total of 756 detected acetylated protein N-termini. We acquired in-depth proteome wide measurements of expression levels of about 2580 proteins. Most remarkably, NatB deletion led to a very significant change in protein phosphorylation.
conclusionsProtein expression levels change only marginally in between WT and nat3Δ. A comparison of the detected NatB substrates with their orthologous revealed remarkably little conservation throughout the phylogenetic tree. We further present evidence of post-translational N-acetylation on protein variants at non-annotated N-termini. Moreover, analysis of downstream effects in nat3Δ revealed elevated protein phosphorylation levels whereby the kinase Snf1p is likely a key element in this process.
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