ArticlePLoS genetics2013
N-alpha-terminal acetylation of histone H4 regulates arginine methylation and ribosomal DNA silencing.
Article in PLoS genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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50 citing papers in PubMed, 74 citations in OpenAlex.
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- Protein acetylation in atherosclerosis: beyond inflammation to core cellular processes and therapeutic potential.Frontiers in immunology · 2026Review
- Mechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatD.Science advances · 2025Article
- Quantitative Top-Down Proteomics Reveals Significant Differences in Histone Proteoforms Between Metastatic and Nonmetastatic Colorectal Cancer Cells.Proteomics · 2025Article
- H2A.X N-terminal acetylation is a newly identified NAA40-mediated modification that is responsive to UV irradiation.Epigenetics & chromatin · 2025Article
- Yeast Nat4 regulates DNA damage checkpoint signaling through its N-terminal acetyltransferase activity on histone H4.PLoS genetics · 2024Article
- Longitudinal adaptive behavioral outcomes in Ogden syndrome by seizure status and therapeutic intervention.American journal of medical genetics. Part A · 2024Article
- N-terminal acetylation of Set1-COMPASS fine-tunes H3K4 methylation patterns.Science advances · 2024Article
- Longitudinal Adaptive Behavioral Outcomes in Ogden Syndrome by Seizure Status and Therapeutic Intervention.medRxiv : the preprint server for health sciences · 2024Article
- Effects of Oncohistone Mutations and PTM Crosstalk on the N-Terminal Acetylation Activities of NatD.ACS chemical biology · 2023Article
- Histone modification inComputational and structural biotechnology journal · 2023Review
- From Nucleus to Membrane: A Subcellular Map of the N-Acetylation Machinery in Plants.International journal of molecular sciences · 2022Review
- Protein Acetylation Going Viral: Implications in Antiviral Immunity and Viral Infection.International journal of molecular sciences · 2022Review
- Research progress on epigenetics of small B-cell lymphoma.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2022Review
- Effects of substrate modifications on the arginine dimethylation activities of PRMT1 and PRMT5.Epigenetics · 2022Article
- Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells.International journal of molecular sciences · 2021Article
- Novel Bisubstrate Inhibitors for Protein N-Terminal Acetyltransferase D.Journal of medicinal chemistry · 2021Article
- N-Terminal Acetyltransferase Naa40p Whereabouts Put into N-Terminal Proteoform Perspective.International journal of molecular sciences · 2021Article
- Identification of NAA40 as a Potential Prognostic Marker for Aggressive Liver Cancer Subtypes.Frontiers in oncology · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational modifications of histones play a key role in DNA-based processes, like transcription, by modulating chromatin structure. N-terminal acetylation is unique among the numerous histone modifications because it is deposited on the N-alpha amino group of the first residue instead of the side-chain of amino acids. The function of this modification and its interplay with other internal histone marks has not been previously addressed. Here, we identified N-terminal acetylation of H4 (N-acH4) as a novel regulator of arginine methylation and chromatin silencing in Saccharomyces cerevisiae. Lack of the H4 N-alpha acetyltransferase (Nat4) activity results specifically in increased deposition of asymmetric dimethylation of histone H4 arginine 3 (H4R3me2a) and in enhanced ribosomal-DNA silencing. Consistent with this, H4 N-terminal acetylation impairs the activity of the Hmt1 methyltransferase towards H4R3 in vitro. Furthermore, combinatorial loss of N-acH4 with internal histone acetylation at lysines 5, 8 and 12 has a synergistic induction of H4R3me2a deposition and rDNA silencing that leads to a severe growth defect. This defect is completely rescued by mutating arginine 3 to lysine (H4R3K), suggesting that abnormal deposition of a single histone modification, H4R3me2a, can impact on cell growth. Notably, the cross-talk between N-acH4 and H4R3me2a, which regulates rDNA silencing, is induced under calorie restriction conditions. Collectively, these findings unveil a molecular and biological function for H4 N-terminal acetylation, identify its interplay with internal histone modifications, and provide general mechanistic implications for N-alpha-terminal acetylation, one of the most common protein modifications in eukaryotes.
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