ArticleFrontiers in plant science2018
Beyond Histones: New Substrate Proteins of Lysine Deacetylases in Arabidopsis Nuclei.
Article in Frontiers in plant science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Unresolved ER stress restricts in vitro plant cell totipotency.Plant cell reports · 2025Article
- Simple and universal function of acetic acid to overcome the drought crisis.Stress biology · 2023Article
- Jasmonates and Histone deacetylase 6 activate Arabidopsis genome-wide histone acetylation and methylation during the early acute stress response.BMC biology · 2022Article
- Nuclear dynamics: Formation of bodies and trafficking in plant nuclei.Frontiers in plant science · 2022Review
- Histone variants and modifications during abiotic stress response.Frontiers in plant science · 2022Review
- Molecular insights into mechanisms underlying thermo-tolerance in tomato.Frontiers in plant science · 2022Review
- Genetic and Physiological Responses to Heat Stress inFrontiers in plant science · 2022Review
- The Arabidopsis PeptideAtlas: Harnessing worldwide proteomics data to create a comprehensive community proteomics resource.The Plant cell · 2021Article
- Central Metabolism in Mammals and Plants as a Hub for Controlling Cell Fate.Antioxidants & redox signaling · 2021Review
- A complex interplay between SAM synthetase and the epigenetic regulator SIN3 controls metabolism and transcription.The Journal of biological chemistry · 2020Article
- Role of Chromatin Architecture in Plant Stress Responses: An Update.Frontiers in plant science · 2020Review
- Histone Modifications Form Epigenetic Regulatory Networks to Regulate Abiotic Stress Response.Plant physiology · 2020Article
- Peptide-Based 2-Aminophenylamide Probes for Targeting Endogenous Class I Histone Deacetylase Complexes.Chembiochem : a European journal of chemical biology · 2019Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The reversible acetylation of lysine residues is catalyzed by the antagonistic action of lysine acetyltransferases and deacetylases, which can be considered as master regulators of their substrate proteins. Lysine deacetylases, historically referred to as histone deacetylases, have profound functions in regulating stress defenses and development in plants. Lysine acetylation of the N-terminal histone tails promotes gene transcription and decondensation of chromatin, rendering the DNA more accessible to the transcription machinery. In plants, the classical lysine deacetylases from the RPD3/HDA1-family have thus far mainly been studied in the context of their deacetylating activities on histones, and their versatility in molecular activities is still largely unexplored. Here we discuss the potential impact of lysine acetylation on the recently identified nuclear substrate proteins of lysine deacetylases from the Arabidopsis RPD3/HDA1-family. Among the deacetylase substrate proteins, many interesting candidates involved in nuclear protein import, transcriptional regulation, and chromatin remodeling have been identified. These candidate proteins represent key starting points for unraveling new molecular functions of the Arabidopsis lysine deacetylases. Site-directed engineering of lysine acetylation sites on these target proteins might even represent a new approach for optimizing plant growth under climate change conditions.
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