ArticleMolecular systems biology2020
Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation.
Article in Molecular systems biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 81 citations in OpenAlex.
- Insights Into the Role of Lysine Acetylation of Non-Histone Proteins in Plant Immunity.Plant, cell & environment · 2026Review
- Rubisco functional integrity requires a dedicated three-step maturation pathway.Science advances · 2026Article
- Histone acetyltransferases as integrative epigenetic regulators of plant abiotic stress responses.Plant cell reports · 2026Review
- Regulatory mechanisms of post-translational modifications on autophagic flux in neurons following ischemic stroke.Molecular biology reports · 2026Review
- HDAC-mediated non-histone deacetylation as a central regulatory network integrating crop growth and stress adaptation.Plant cell reports · 2026Review
- Article
- NAA10 (N-Alpha-Acetyltransferase 10): A Multifunctional Regulator in Development, Disease, and Cancer.Cells · 2025Review
- Lysine acetylation in cyanobacteria: emerging mechanisms and functions.Biochemical Society transactions · 2025Review
- Illuminating the impact of N-terminal acetylation: from protein to physiology.Nature communications · 2025Review
- Naa80 is required for actin N-terminal acetylation and normal hearing in zebrafish.Life science alliance · 2024Article
- Distribution and diversity of classical deacylases in bacteria.Nature communications · 2024Article
- Intra-chloroplast proteases: A holistic network view of chloroplast proteolysis.The Plant cell · 2024Review
- The lowdown on breakdown: Open questions in plant proteolysis.The Plant cell · 2024Review
- Dynamic microfluidic single-cell screening identifies pheno-tuning compounds to potentiate tuberculosis therapy.Nature communications · 2024Article
- Nt-acetylation-independent turnover of SQUALENE EPOXIDASE 1 by Arabidopsis DOA10-like E3 ligases.Plant physiology · 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
- Loss of Chloroplast GNAT Acetyltransferases Results in Distinct Metabolic Phenotypes in Arabidopsis.Plant & cell physiology · 2023Article
- Remodeling of algal photosystem I through phosphorylation.Bioscience reports · 2023Article
- The Global Acetylation Profiling Pipeline for Quick Assessment of Protein N-Acetyltransferase Specificity In Cellulo.Methods in molecular biology (Clifton, N.J.) · 2023Article
- From Nucleus to Membrane: A Subcellular Map of the N-Acetylation Machinery in Plants.International journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
22 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N-α-acetylation (NTA) and ε-lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5-related N-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA specificities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid proteins, while proteins of other compartments were unaffected. The data indicate that these enzymes have specific protein targets and likely display partly redundant selectivity, increasing the robustness of the acetylation process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzymatic activities.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.