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:The regulation of stomatal aperture in plants is impacted by changes in hormones and the environment and is controlled by a complex signaling cascade within guard cells. Mitochondria and chloroplast play a crucial role in regulating reactive oxygen species (ROS) production in plants, which also triggers stomatal movement. However, the regulation of ROS production in mitochondria and chloroplasts still need to be addressed. Abscisic acid (ABA) stimulates ROS production in guard cells, leading to stomatal closure during drought stress. Transcriptomic analysis in Arabidopsis reveals increased expression of ROS-inducing proteins NADPH oxidases and decreased expression of ROS scavengers, including mitochondrial complex I and III. The mechanism regulating ROS inducers and scavengers during ABA and drought stress remains unclear. Our study proposes epigenetic regulation of the mitochondria and chloroplast proteins by Histone deacetylase 9 (HDA9). Loss of function mutant hda9-1 displays ABA insensitivity, representing HDA9's negative regulation in ABA stress. Transcriptomic analysis of hda9-1 also shows increased expression of cytochrome C oxidase-like protein thioredoxin M-4 and ferrdoxin-1, and decreased expression of NADPH oxidases, in contrast to wild-type plants. ChIP-seq analysis using anti HDA9-FLAG antibodies reveals enrichment of cytochrome C oxidase-like protein, thioredoxin M-4, and ferrdoxin-1 loci. Our data suggest that HDA9 binds to these loci on the chromatin and represses their transcription in response to ABA stress.
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