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POWERDRESS interacts with HISTONE DEACETYLASE 9 to promote aging in Arabidopsis

ABSTRACT: Functional analysis of HDA9 in Arabidopsis

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE80056 | GEO | 2016/11/11

SECONDARY ACCESSION(S): PRJNA317722

REPOSITORIES: GEO

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POWERDRESS interacts with HISTONE DEACETYLASE 9 to promote aging in Arabidopsis.

Project description:Leaf senescence is an essential part of the plant lifecycle during which nutrients are re-allocated to other tissues. The regulation of leaf senescence is a complex process. However, the underlying mechanism is poorly understood. Here, we uncovered a novel and the pivotal role of Arabidopsis HDA9 (a RPD3-like histone deacetylase) in promoting the onset of leaf senescence. We found that HDA9 acts in complex with a SANT domain-containing protein POWERDRESS (PWR) and transcription factor WRKY53. Our genome-wide profiling of HDA9 occupancy reveals that HDA9 directly binds to the promoters of key negative regulators of senescence and this association requires PWR. Furthermore, we found that PWR is important for HDA9 nuclear accumulation. This study reveals an uncharacterized epigenetic complex involved in leaf senescence and provides mechanistic insights into how a histone deacetylase along with a chromatin-binding protein contribute to a robust regulatory network to modulate the onset of plant aging.

| S-EPMC5119886 | biostudies-literature

Regulation of histone deacetylase activity by serine phosphorylation conserved in Arabidopsis and human

Project description:In this study, we uncovered a novel phosphorylation site that plays pivotal roles in regulating the activity of Arabidopsis HDA9 and human HDAC3

2024-09-16 | GSE243403 | GEO

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

Comparison of histone deacetylase 9-1 mutant (SALK_001723) dry seed transcriptome with Col wild-type

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Comparison of histone deacetylase 9-1 mutant (SALK_001723) dry seed transcriptome with Col wild-type

Project description:Analysis of the transcriptome of dry hda9-1 mutant seeds with those of Col wild-type seeds, using Affymetrix GeneChip Arabidopsis ATH1 Genome Array. The hda9-1 mutant has reduced primary seed dormancy. We used microarrays to dissect which genes are differentially expressed in the hda9-1 mutant to study the mechanisms how HDA9 affects seed dormancy and germination RNA was extracted from tagged dry 18-19-DAP siliques of wild-type Col and the hda9-1 mutant following an adapted protocol of the RNAqueous small scale Phenol-free total RNA isolation kit in addition with RNA isolation aid (Ambion, Austing, TX, USA), as described in Liu et al. (2011) PLoS ONE and Van Zanten et al. (2011) PNAS. Affymetrix GeneChip Arabidopsis ATH1 Genome-Micro hybridization was performed at the Max Planck Genome Centre Cologne. Three independent hybridizations of independent biological replicates, obtained from several dry siliques of at least five plants per replica, were performed.

2014-09-21 | E-GEOD-50786 | biostudies-arrayexpress

HOS15 interacts with a histone deacetylase to control gene expression and development

Project description:This study identified HOS15, a protein with a WD40-repeat, as an interactor with the HDA9-PWR histone deacetalyse complex. HOS15 has an essential role in controlling HDA9-specific gene expression and development.

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A light signaling factor, ELONGATED HYPOCOTYL 5 (HY5) interacts with Histone deacetylase 9 (HDA9) to play a suppressive role in the glucosinolate biosynthesis in Arabidopsis

Project description:In this study, we found that a light signaling factor, Long Hypocotyl 5 (HY5) is closely involved in the regulation of GSLs contents in light condition. In addition, HY5 was shown to physically interact with a histone deacetylase HDA9 and bind to proximal promoter region of MYB29 and IMD1 to suppress aliphatic GSL biosynthetic process. These results demonstrate that HY5 acts to suppress GSL accumulation at daytime, thus properly modulating the GSL contents on a daily basis of Arabidopsis plant.

2024-06-12 | GSE250418 | GEO

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

Arabidopsis sp. hda9-2

Project description:Arabidopsis hda9-2 raw sequence reads

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