ArticleNucleic acids research2021
Histone deacetylases control lysine acetylation of ribosomal proteins in rice.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.
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Who cites it
40 citing papers in PubMed, 1 synthesis or guideline pooled it, 86 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
- Insights Into the Role of Lysine Acetylation of Non-Histone Proteins in Plant Immunity.Plant, cell & environment · 2026Review
- Roles and Mechanisms of Histone Deacetylases in Plant Abiotic Stress Responses.Antioxidants (Basel, Switzerland) · 2026Review
- Ribosome Heterogeneity in Plants: The Causes of This Phenomenon and Its Implications on Gene Expression.Plants (Basel, Switzerland) · 2026Review
- Landscape of protein S-palmitoylation and its role in suppressing cytosolic translation under cold stress in rice.Plant communications · 2026Article
- HDAC-mediated non-histone deacetylation as a central regulatory network integrating crop growth and stress adaptation.Plant cell reports · 2026Review
- Insects manipulate host nuclear trafficking and epigenetic regulation to facilitate herbivory.Nature communications · 2026Article
- Lysine β-hydroxybutyrylation as a drought-responsive epigenetic mark in rice.Cell discovery · 2026Article
- Reciprocal control of metabolic and chromatin regulators improves rice tolerance to heat.Nature communications · 2025Article
- The role of post-translational modifications in the dynamics of cytoplasmic biomolecular condensates in plants.The New phytologist · 2025Review
- Unresolved ER stress restricts in vitro plant cell totipotency.Plant cell reports · 2025Article
- Identification of Rice LncRNAs and Their Roles in the Rice Blast Resistance Network Using Transcriptome and Translatome.Plants (Basel, Switzerland) · 2025Article
- Regulation of mNature plants · 2025Article
- Genome-wide identification of theFrontiers in plant science · 2025Article
- Menthone lowers H3K27ac levels to inhibitFrontiers in microbiology · 2025Article
- Versatile plant genome engineering using anti-CRISPR-Cas12a systems.Science China. Life sciences · 2024Article
- Advances in understanding the roles of plant HAT and HDAC in non-histone protein acetylation and deacetylation.Planta · 2024Review
- Comparative Proteomics and Metabonomics Analysis of Different Diapause Stages Revealed a New Regulation Mechanism of Diapause inMolecules (Basel, Switzerland) · 2024Article
- ESR2-HDA6 complex negatively regulates auxin biosynthesis to delay callus initiation in Arabidopsis leaf explants during tissue culture.Plant communications · 2024Article
- The crotonylated and succinylated proteins of jujube involved in phytoplasma-stress responses.BMC biology · 2024Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lysine acetylation (Kac) is well known to occur in histones for chromatin function and epigenetic regulation. In addition to histones, Kac is also detected in a large number of proteins with diverse biological functions. However, Kac function and regulatory mechanism for most proteins are unclear. In this work, we studied mutation effects of rice genes encoding cytoplasm-localized histone deacetylases (HDAC) on protein acetylome and found that the HDAC protein HDA714 was a major deacetylase of the rice non-histone proteins including many ribosomal proteins (r-proteins) and translation factors that were extensively acetylated. HDA714 loss-of-function mutations increased Kac levels but reduced abundance of r-proteins. In vitro and in vivo experiments showed that HDA714 interacted with r-proteins and reduced their Kac. Substitutions of lysine by arginine (depleting Kac) in several r-proteins enhance, while mutations of lysine to glutamine (mimicking Kac) decrease their stability in transient expression system. Ribo-seq analysis revealed that the hda714 mutations resulted in increased ribosome stalling frequency. Collectively, the results uncover Kac as a functional posttranslational modification of r-proteins which is controlled by histone deacetylases, extending the role of Kac in gene expression to protein translational regulation.
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