ArticleProceedings of the National Academy of Sciences of the United States of America2016
POWERDRESS and HDA9 interact and promote histone H3 deacetylation at specific genomic sites in Arabidopsis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 107 citations in OpenAlex.
- TONSOKU prevents the formation of large tandem duplications and restrains ATR-WEE1 checkpoint activation.Nature communications · 2026Article
- HOS15 together with PWR-HDA9 positively regulates dark-induced senescence in Arabidopsis.Plant signaling & behavior · 2025Article
- The SNL Histone Deacetylase-Binding Factor GmHE13 Is a Novel Regulator of Soybean Hypocotyl Elongation.Plant biotechnology journal · 2025Article
- Insights into the roles of chromatin-remodeling complex HOS15-PWR-HDA9 in plant development and stress responses.Plant cell reports · 2025Review
- Genome scans capture key adaptation and historical hybridization signatures in tetraploid wheat.The plant genome · 2025Article
- Epigenetics and plant hormone dynamics: a functional and methodological perspective.Journal of experimental botany · 2024Review
- Complex Polyploids: Origins, Genomic Composition, and Role of Introgressed Alleles.Systematic biology · 2024Article
- An epigenetic timer regulates the transition from cell division to cell expansion during Arabidopsis petal organogenesis.PLoS genetics · 2024Article
- Structure-function analyses revealCurrent research in structural biology · 2024Article
- Article
- POWERDRESS positively regulates systemic acquired resistance in Arabidopsis.Plant cell reports · 2022Article
- HDAC3 Knockdown Dysregulates Juvenile Hormone and Apoptosis-Related Genes inInternational journal of molecular sciences · 2022Article
- HISTONE DEACETYLASE 9 transduces heat signal in plant cells.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- PICKLE associates with histone deacetylase 9 to mediate vegetative phase change in Arabidopsis.The New phytologist · 2022Article
- Review
- Epigenetic regulation of thermomorphogenesis inaBIOTECH · 2022Review
- Epigenetic control of abiotic stress signaling in plants.Genes & genomics · 2022Review
- Programming changes of hippocampal miR-134-5p/SOX2 signal mediate the susceptibility to depression in prenatal dexamethasone-exposed female offspring.Cell biology and toxicology · 2022Article
- Negative regulation of floral transition in Arabidopsis by HOS15-PWR-HDA9 complex.Frontiers in plant science · 2022Article
- Mysteries of gene regulation: Promoters are not the sole triggers of gene expression.Computational and structural biotechnology journal · 2022Article
Corrections and comments
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Authors and funding
13 authors at 7 institutions in 3 countries.
Funding
Abstract
Histone acetylation is a major epigenetic control mechanism that is tightly linked to the promotion of gene expression. Histone acetylation levels are balanced through the opposing activities of histone acetyltransferases (HATs) and histone deacetylases (HDACs). Arabidopsis HDAC genes (AtHDACs) compose a large gene family, and distinct phenotypes among AtHDAC mutants reflect the functional specificity of individual AtHDACs However, the mechanisms underlying this functional diversity are largely unknown. Here, we show that POWERDRESS (PWR), a SANT (SWI3/DAD2/N-CoR/TFIII-B) domain protein, interacts with HDA9 and promotes histone H3 deacetylation, possibly by facilitating HDA9 function at target regions. The developmental phenotypes of pwr and hda9 mutants were highly similar. Three lysine residues (K9, K14, and K27) of H3 retained hyperacetylation status in both pwr and hda9 mutants. Genome-wide H3K9 and H3K14 acetylation profiling revealed elevated acetylation at largely overlapping sets of target genes in the two mutants. Highly similar gene-expression profiles in the two mutants correlated with the histone H3 acetylation status in the pwr and hda9 mutants. In addition, PWR and HDA9 modulated flowering time by repressing AGAMOUS-LIKE 19 expression through histone H3 deacetylation in the same genetic pathway. Finally, PWR was shown to physically interact with HDA9, and its SANT2 domain, which is homologous to that of subunits in animal HDAC complexes, showed specific binding affinity to acetylated histone H3. We therefore propose that PWR acts as a subunit in a complex with HDA9 to result in lysine deacetylation of histone H3 at specific genomic targets.
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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.