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POWERDERESS and HDA9 interact and promote histone H3 deacetylation at specific lysine residues in Arabidopsis.

ABSTRACT: POWERDERESS and HDA9 interact and promote histone H3 deacetylation at specific lysine residues in Arabidopsis.

PROVIDER: PRJNA353120 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR5011160_1.fastq.gz	Fastqsanger.gz
	SRR5011160_2.fastq.gz	Fastqsanger.gz
	SRR5011170.fastq.gz	Fastqsanger.gz
	SRR5011180.fastq.gz	Fastqsanger.gz
	SRR5011161_1.fastq.gz	Fastqsanger.gz

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POWERDERESS and HDA9 interact and promote histone H3 deacetylation at specific lysine residues in Arabidopsis. [RNA-Seq]

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

POWERDERESS and HDA9 interact and promote histone H3 deacetylation at specific lysine residues in Arabidopsis. [ChIP-Seq]

2017-01-25 | GSE89768 | GEO

POWERDERESS and HDA9 interact and promote histone H3 deacetylation at specific lysine residues in Arabidopsis.

Project description:This SuperSeries is composed of the SubSeries listed below.

2017-01-25 | GSE89770 | GEO

POWERDRESS and HDA9 interact and promote histone H3 deacetylation at specific genomic sites in Arabidopsis.

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 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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Arabidopsis thaliana

Project description:POWERDERESS and HDA9 interact and promote histone H3 deacetylation at specific lysine residues in Arabidopsis. [ChIP-Seq]

| PRJNA353121 | ENA

Arabidopsis thaliana

Project description:POWERDERESS and HDA9 interact and promote histone H3 deacetylation at specific lysine residues in Arabidopsis. [RNA-Seq]

| PRJNA353122 | ENA

The Histone Deacetylases HDA6 and HDA9 coordinately regulate valve cell elongation through depressing auxin signaling in Arabidopsis

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.

2018-12-30 | GSE122047 | GEO

HOS15 and HDA9 negatively regulate immunity through histone deacetylation on intracellular immune receptor NLR genes in Arabidopsis

Project description:HOS15 and HDA9 negatively regulate immunity through histone deacetylation on intracellular immune receptor NLR genes in Arabidopsis

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Vp1524, a Vibrio parahaemolyticus NAD+ dependent deacetylase, regulates host response during infection by induction of histone deacetylation

Project description:Here we report V. parahaemolyticus (serotype O3:K6) infection induced histone deacetylation in intestinal epithelial cells, wherein we have shown deacetylation of H3K9, H3K56, H3K18 and H4K16 residues. Interestingly we observed concomitant downregulation of host deacetylases.

2021-09-22 | GSE158369 | GEO

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