ArticleNature plants2024
Lysine acetylation of histone acetyltransferase adaptor protein ADA2 is a mechanism of metabolic control of chromatin modification in plants.
Article in Nature plants, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.
- Acetylation as a dynamic regulatory interface between plant stress memory, cross-tolerance, and crop resilience design.Frontiers in plant science · 2026Pooled it
- Linking cellular metabolism to chromatin modifications in plants.Journal of integrative plant biology · 2026Review
- Direct and high-yield chromatin isolation by SBCP unlocks superior plant proteomics and epigenomic profiling.Plant cell reports · 2026Article
- Histone acetyltransferases as integrative epigenetic regulators of plant abiotic stress responses.Plant cell reports · 2026Review
- Lysine acetylome analysis reveals the critical role of acetylation-modified transcription factors and a chaperone protein in regulation of salt tolerance in Tamarix hispida.BMC plant biology · 2026Article
- Transcriptional adapter ADA2 regulates yield and end-use quality through liquid-liquid phase separation in wheat.Journal of integrative plant biology · 2026Article
- Research Progress on Histone Modification Regulation Mechanisms and Breeding Applications in Plant Abiotic Stress Responses.Plants (Basel, Switzerland) · 2026Review
- Glycolytic lactylation modulates cell death decisions in diabetic kidney disease: Metabolic‑epigenetic interplay between ferroptosis and autophagy in fibrotic remodeling (Review).International journal of molecular medicine · 2026Review
- RNA modifications and epigenetic regulation in plants.aBIOTECH · 2026Review
- The Transcription Factor FgSge1 Harnesses the SAGA Complex to Activate Mycotoxin Biosynthesis and Fungal Virulence.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- KMT2C Loss Promotes NF2-Wildtype Meningioma Progression and Ferroptosis Sensitivity via Epigenetic Repression of Hippo Signaling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Dynamic chromatin regulatory programs of sucrose and citric acid metabolism during fruit ripening in Citrus.The Plant cell · 2026Article
- ADA2 Forms Nuclear Condensates with GCN5 and ATP-Citrate Lyase (ACL) to Modulate H3K9 Acetylation at Genes Functioning in Rice Meristems.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Identification of DNA Methyltransferase/Demethylase Genes and 5-Azacytidine's Impact on β-Elemene and Methylation inBiology · 2025Article
- The plant epigenome governed by nutrients and metabolism.Current opinion in plant biology · 2025Review
- Reciprocal control of metabolic and chromatin regulators improves rice tolerance to heat.Nature communications · 2025Article
- Regulation of mNature plants · 2025Article
- Redox signalling in the nucleus: shaping the epigenetic code.Journal of experimental botany · 2025Article
- Adaptable Alchemy: Exploring the Flexibility of Specialized Metabolites to Environmental Perturbations Through Post-Translational Modifications (PTMs).Plants (Basel, Switzerland) · 2025Review
- Advances in understanding the roles of plant HAT and HDAC in non-histone protein acetylation and deacetylation.Planta · 2024Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Histone acetylation is a predominant active chromatin mark deposited by histone acetyltransferases (HATs) that transfer the acetyl group from acetyl coenzyme A (acetyl-CoA) to lysine ε-amino groups in histones. GENERAL CONTROL NON-REPRESSED PROTEIN 5 (GCN5) is one of the best-characterized HATs and functions in association with several adaptor proteins such as ADA2 within multiprotein HAT complexes. ADA2-GCN5 interaction increases GCN5 binding to acetyl-CoA and stimulates its HAT activity. It remains unclear whether the HAT activity of GCN5 (which acetylates not only histones but also cellular proteins) is regulated by acetyl-CoA levels, which vary greatly in cells under different metabolic and nutrition conditions. Here we show that the ADA2 protein itself is acetylated by GCN5 in rice cells. Lysine acetylation exposes ADA2 to a specific E3 ubiquitin ligase and reduces its protein stability. In rice plants, ADA2 protein accumulation reversely parallels its lysine acetylation and acetyl-CoA levels, both of which are dynamically regulated under varying growth conditions. Stress-induced ADA2 accumulation could stimulate GCN5 HAT activity to compensate for the reduced acetyl-CoA levels for histone acetylation. These results indicate that ADA2 lysine acetylation that senses cellular acetyl-CoA variations is a mechanism to regulate HAT activity and histone acetylation homeostasis in plants under changing environments.
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