Arabidopsis sp. hda9-2
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA299441 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR2757693.fastq.gz | Fastqsanger.gz | |||
| SRR2756974.fastq.gz | Fastqsanger.gz |
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Project description: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 positive regulator of floral stem cell maintenance, interacts with HDA9 and promotes histone H3 deacetylation possibly by facilitating HDA9 function at target chromatin. The PWR SANT2 domain, which is homologous to that of subunits in animal HDAC complexes, showed specific binding affinity to acetylated histone H3. Three lysine residues (K9, K14 and K27) of H3 retained hyperacetylation status in both pwr and hda9 mutants. Genome wide H3K9 and H3K14 acetylation levels were generally elevated, and a large portion of acetylated targets overlapped between the pwr and hda9 mutants. Comparative analysis revealed a correlation between gene expression and histone H3 acetylation status in the pwr and hda9 mutants. In addition, PWR and HDA9 modulated the AGAMOUS-LIKE 19 (AGL19)-mediated flowering time pathway through histone H3 deacetylation. Finally, PWR was shown to physically interact with HDA9. We therefore propose that PWR acts as a subunit in a complex with HDA9 to negatively regulate the acetylation of specific lysine residues of histone H3 at genomic targets.
2017-01-25 | GSE89768 | GEO
Project description: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 positive regulator of floral stem cell maintenance, interacts with HDA9 and promotes histone H3 deacetylation possibly by facilitating HDA9 function at target chromatin. The PWR SANT2 domain, which is homologous to that of subunits in animal HDAC complexes, showed specific binding affinity to acetylated histone H3. Three lysine residues (K9, K14 and K27) of H3 retained hyperacetylation status in both pwr and hda9 mutants. Genome wide H3K9 and H3K14 acetylation levels were generally elevated, and a large portion of acetylated targets overlapped between the pwr and hda9 mutants. Comparative analysis revealed a correlation between gene expression and histone H3 acetylation status in the pwr and hda9 mutants. In addition, PWR and HDA9 modulated the AGAMOUS-LIKE 19 (AGL19)-mediated flowering time pathway through histone H3 deacetylation. Finally, PWR was shown to physically interact with HDA9. We therefore propose that PWR acts as a subunit in a complex with HDA9 to negatively regulate the acetylation of specific lysine residues of histone H3 at genomic targets.
2017-01-25 | GSE89769 | GEO
Project description:Both of Histone Deacetylases HDA6 and HDA9 belong to RPD3/HDA1 class I subfamily, and they have similar protein structure. Loss of function of HDA9 display a blunt silique. Although there is not protein-protein interaction between HDA6 and HDA9, they simultaneously loss function led to “nock-shape” silique that more seriously silique phenotype than hda9. The silique valve cell of hda9 and hda6 hda9 were longer than wild type and hda6. The transcripts level of auxin signaling related genes were mis-regulated in hda9 and hda6 hda9 silique, and GFP signaling derived by auxin response promoter DR5 were weaker in hda9 and hda6 hda9 than wild type and hda6. Thus, our findings reveal that HDA6 and HDA9 coordinately control silique valve cell elongation through affecting auxin signaling related genes expression in silique.
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Project description:Many plants, including Arabidopsis thaliana, respond to elevated ambient temperatures by altering their growth through a process known as thermomorphogenesis. This response involves the depletion of the repressive histone variant H2A.Z from the gene bodies of PIF4-regulated auxin-related genes, enabling their transcriptional activation. Interestingly, this activation also requires the histone deacetylase HDA9, raising the question of how histone deacetylation, typically associated with transcriptional repression, can instead promote gene activation. Here, we identify FVE as a co-regulator that partners with HDA9 to activate PIF4 target genes at elevated temperatures. PIF4 directly interacts with and recruits the FVE-HDA9 complex to its target genes to remove acetylation from histone H4 and H2A.Z. We show that H2A.Z acetylation is required for recruiting the SWR1 complex, which deposits H2A.Z. Consequently, FVE-HDA9-mediated deacetylation reduces SWR1 complex binding and limits H2A.Z deposition. Moreover, we demonstrate that in addition to limiting H2A.Z deposition, H2A.Z depletion also results from H2A.Z eviction mediated by the INO80 complex. Together, these findings uncover a dual mechanism contributing to H2A.Z depletion: INO80-mediated active eviction and histone deacetylation-mediated inhibition of H2A.Z deposition, which underlies PIF4 target gene activation and explain the paradoxical role of histone deacetylation in transcriptional activation.
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