Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Perturbation of the relative abundance of H2A.Z variants alters H3K27me3 enrichment in Arabidopsis thaliana [ChIP-Seq]

ABSTRACT: H3K27me3 is a histone modification associated with transcriptional repression that plays a pivotal role in differentiation and development in plants and animals. H2A.Z, a histone variant of H2A, is often colocalized with H3K27me3 in Arabidopsis. Previous genome-wide studies have raised the possibility that H2A.Z contributes to H3K27me3 homeostasis in plants. To examine the contribution of H2A.Z to H3K27me3, we made use of hta9 hta11, a plant line which is defective in two of three genes that code for H2A.Z and which has been previously characterized as an H2A.Z-depletion mutant. Surprisingly, ChIP-seq analysis of H2A.Z enrichment revealed that hta9 hta11 plants exhibit a nearly indistinguishable genic H2A.Z enrichment pattern relative to wild type with few genes that are differentially enriched for H2A.Z. Mass spectrometry measurement of histone abundance in hta9 hta11 plants in conjunction with our ChIP-seq analysis indicates that the chromatin of hta9 hta11 plants exhibits altered relative abundance of H2A.Z variants rather than a global depletion of H2A.Z. In contrast, ChIP-seq analysis of H3K27me3 reveals that hta9 hta11 plants exhibit a robustly global reduction in H3K27me3 enrichment, and numerous genes are identified that exhibit altered levels for H3K27me3. In addition, hta9 hta11 plants exhibit differential expression of thermoresponsive genes that have previously been shown to be dependent on H2A.Z. Our combined analyses indicate that specific H2A.Z isoforms play distinct roles in chromatin composition and gene expression in Arabidopsis, particularly with regards to H3K27me3 homeostasis.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE282947 | GEO | 2026/08/04

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Perturbation of the relative abundance of H2A.Z variants alters H3K27me3 enrichment in Arabidopsis thaliana - Untargeted Analysis

Project description:H3K27me3 is a histone modification associated with transcriptional repression that plays a pivotal role in differentiation and development in plants and animals. H2A.Z, a histone variant of H2A, is often colocalized with H3K27me3 in Arabidopsis. Previous genome-wide studies have raised the possibility that H2A.Z contributes to H3K27me3 homeostasis in plants. To examine the contribution of H2A.Z to H3K27me3, we utilized hta9 hta11, a plant line which is defective in two of three genes that code for H2A.Z and has been previously characterized as an H2A.Z-depletion mutant. Surprisingly, ChIP-seq analysis of H2A.Z enrichment revealed that hta9 hta11 plants exhibit a nearly indistinguishable genic H2A.Z enrichment pattern relative to wild type with few genes that are enriched or depleted for H2A.Z. Mass spectrometry measurement of histone protein abundance in hta9 hta11 plants in conjunction with our ChIP-seq analysis indicates that the chromatin of hta9 hta11 plants exhibits altered relative abundance of H2A.Z variants rather than a global depletion of H2A.Z. In contrast, ChIP-seq analysis of H3K27me3 reveals that hta9 hta11 plants exhibit a robust global reduction in H3K27me3 enrichment, and numerous genes are identified that exhibit altered levels for H3K27me3. In addition, hta9 hta11 plants exhibit differential expression of thermoresponsive genes that have previously been shown to be dependent on H2A.Z. Our combined analyses indicate that specific H2A.Z isoforms play distinct roles in chromatin composition and gene expression in Arabidopsis, particularly with regards to H3K27me3 homeostasis.

2026-08-03 | PXD058289 | Pride

Perturbation of the relative abundance of H2A.Z variants alters H3K27me3 enrichment in Arabidopsis thaliana [RNA-Seq]

Project description:H3K27me3 is a histone modification associated with transcriptional repression that plays a pivotal role in differentiation and development in plants and animals. H2A.Z, a histone variant of H2A, is often colocalized with H3K27me3 in Arabidopsis. Previous genome-wide studies have raised the possibility that H2A.Z contributes to H3K27me3 homeostasis in plants. To examine the contribution of H2A.Z to H3K27me3, we made use of hta9 hta11, a plant line which is defective in two of three genes that code for H2A.Z and which has been previously characterized as an H2A.Z-depletion mutant. Surprisingly, ChIP-seq analysis of H2A.Z enrichment revealed that hta9 hta11 plants exhibit a nearly indistinguishable genic H2A.Z enrichment pattern relative to wild type with few genes that are differentially enriched for H2A.Z. Mass spectrometry measurement of histone abundance in hta9 hta11 plants in conjunction with our ChIP-seq analysis indicates that the chromatin of hta9 hta11 plants exhibits altered relative abundance of H2A.Z variants rather than a global depletion of H2A.Z. In contrast, ChIP-seq analysis of H3K27me3 reveals that hta9 hta11 plants exhibit a robustly global reduction in H3K27me3 enrichment, and numerous genes are identified that exhibit altered levels for H3K27me3. In addition, hta9 hta11 plants exhibit differential expression of thermoresponsive genes that have previously been shown to be dependent on H2A.Z. Our combined analyses indicate that specific H2A.Z isoforms play distinct roles in chromatin composition and gene expression in Arabidopsis, particularly with regards to H3K27me3 homeostasis.

2026-08-04 | GSE282948 | GEO

Perturbation of the relative abundance of H2A.Z variants alters H3K27me3 enrichment in Arabidopsis thaliana

| PXD058581 | panorama

Replacement of Arabidopsis H2A.Z with human H2A.Z orthologs reveals extensive functional conservation and limited importance of the N-terminal tail sequence for Arabidopsis development (ChIP-Seq)

Project description:To investigate the functional conservation of H2A.Z histones during eukaryotic evolution we transformed h2a.z deficient plants with three human H2A.Z proteins to assess their ability to rescue the mutant defects. We discovered that human H2A.Z.1 and H2A.Z.2.1 fully complement the phenotypic abnormalities of h2a.z plants even though Arabidopsis and human H2A.Z N-terminal tail sequences are divergent, while the brain-specific splice variant H2A.Z.2.2 has a dominant-negative effect in wild-type plants. Furthermore, H2A.Z.1 almost completely re-establishes normal H2A.Z chromatin occupancy in h2a.z plants and restores the expression of more than 84 % of misexpressed genes. Finally, our hypothesis that the N-terminal tail of Arabidopsis H2A.Z is not crucial for its overall function was supported by the ability of N-terminal end truncations of Arabidopsis HTA11 to largely rescue the defects of h2a.z mutants.

2024-05-13 | GSE263312 | GEO

Replacement of Arabidopsis H2A.Z with human H2A.Z orthologs reveals extensive functional conservation and limited importance of the N-terminal tail sequence for Arabidopsis development (WT, h2a.z + HsH2A.Z. RNA-Seq)

2024-05-13 | GSE263311 | GEO

2024-05-13 | GSE263310 | GEO

Perturbation of the relative abundance of H2A.Z variants alters H3K27me3 enrichment in Arabidopsis thaliana [ChIP-Seq]

Project description:Perturbation of the relative abundance of H2A.Z variants alters H3K27me3 enrichment in Arabidopsis thaliana [ChIP-Seq]

| PRJNA1191142 | ENA

Major waves of H2A.Z incorporation during mouse oogenesis and preimplantation embryo development

Project description:Epigenomes of mammalian oocytes and embryos undergo major transitions essential for successful development. Here, we provide genome-wide maps of histone variant H2A.Z during twelve stages of mouse oogenesis and preimplantation embryo development and relate it to histone marks and genomic features. This revealed that major waves of H2A.Z incorporation occur early in growing oocytes, forming distinct patterns of maternal, embryonic, and persistent H2A.Z enrichment. Late maternal enrichment is inherited by the zygote, and precedes reduced formation of lamina associated domains and early replication in the maternal genome of 2-cell embryos. Persistent H2A.Z enrichment is strongly associated with CpG islands and H3K4me3 near transcription start sites of active genes, but thousands of maternal and embryonic H2A.Z incorporation sites exist elsewhere, frequently at transposable elements. The persisting H2A.Z enrichments across related developmental stages enable preservation of epigenetic information despite major concurrent changes in H3K4me3, H3K27me3, and DNA methylation. Altogether, this advances our understanding of how histone variants contribute to epigenetic reprogramming during mammalian oogenesis and early development.

2025-11-04 | GSE293415 | GEO

Project description:In eukaryotes, DNA wraps around histones to form nucleosomes, which are compacted into chromatin. DNA-templated processes, including transcription, require chromatin disassembly and reassembly mediated by histone chaperones. Additionally, distinct histone variants can replace core histones to regulate chromatin structure and function. Although replacement of H2A with the evolutionarily conserved H2A.Z via the SWR1 histone chaperone complex has been extensively studied, in plants little is known about how a reduction of H2A.Z levels can be achieved. Here, we show that NRP proteins cause a decrease of H2A.Z-containing nucleosomes in Arabidopsis under standard growing conditions. nrp1-1 nrp2-2 double mutants show an over-accumulation of H2A.Z genome-wide, especially at heterochromatic regions normally H2A.Z-depleted in wild-type plants. Our work suggests that NRP proteins regulate gene expression by counteracting SWR1, thereby preventing excessive accumulation of H2A.Z.

2020-05-18 | PXD019248 | Pride

Perturbation of the relative abundance of H2A.Z variants alters H3K27me3 enrichment in Arabidopsis thaliana [RNA-Seq]

Project description:Perturbation of the relative abundance of H2A.Z variants alters H3K27me3 enrichment in Arabidopsis thaliana [RNA-Seq]

| PRJNA1191141 | ENA