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The histone acetylation module and histone chaperone in the Arabidopsis NuB4 complex have synergistic effect on chromatin accessibility

ABSTRACT: The histone acetylation module and histone chaperone in the Arabidopsis NuB4 complex have synergistic effect on chromatin accessibility

PROVIDER: PRJNA1081443 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR28125326_1.fastq.gz	Fastqsanger.gz
	SRR28125326_2.fastq.gz	Fastqsanger.gz
	SRR28125327_1.fastq.gz	Fastqsanger.gz
	SRR28125327_2.fastq.gz	Fastqsanger.gz
	SRR28125328_1.fastq.gz	Fastqsanger.gz

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The histone acetylation module and histone chaperone in the Arabidopsis NuB4 complex have synergistic effect on chromatin accessibility (ChIP-Seq)

Project description:Although the conserved type B histone acetyltransferase is known to regulate both cytoplasmic histone acetylation and nuclear nucleosome assembly, the coordination between the dual functions remains poorly understood. Our study revealed that the Arabidopsis thaliana type B histone acetyltransferase HAG2 interactions with the histone chaperones MSI2, MSI3, and NASP, as well as histones H3 and H4, resulting in the formation of a conserved NuB4 complex. Within this complex, HAG2, MSI2, and MSI3 constitute a histone acetylation module that acetylates newly synthesized histone H4 at lysine 5 and 12 sites in the cytoplasm. This module collaborates with NASP to maintain the abundance of H3 and H4 proteins in the cytoplasm, but it is not necessary for nucleosome assembly in the nucleus, which differs from the role of NuB4 complexes in other eukaryotes. Furthermore, we found that, within the nucleus, the collaborative actions of the histone acetylation module and NASP enhance chromatin accessibility near the transcription start sites of protein-coding genes, while showing a negative impact on chromatin accessibility near the transcription termination sites. This suggests that the Arabidopsis NuB4 complex is responsible for modulating chromatin accessibility across the entire genome, highlighting a plant-specific function of the NuB4 complex.

2024-10-25 | GSE259414 | GEO

The histone acetylation module and histone chaperone in the Arabidopsis NuB4 complex have synergistic effect on chromatin accessibility (ATAC-Seq)

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The histone acetylation module and histone chaperone in the Arabidopsis NuB4 complex have synergistic effect on chromatin accessibility (RNA-Seq)

2024-10-25 | GSE259415 | GEO

The histone acetylation module and histone chaperone in the Arabidopsis NuB4 complex have synergistic effect on chromatin accessibility (RNA-Seq)

Project description:The histone acetylation module and histone chaperone in the Arabidopsis NuB4 complex have synergistic effect on chromatin accessibility (RNA-Seq)

| PRJNA1081445 | ENA

The histone acetylation module and histone chaperone in the Arabidopsis NuB4 complex have synergistic effect on chromatin accessibility (ChIP-Seq)

Project description:The histone acetylation module and histone chaperone in the Arabidopsis NuB4 complex have synergistic effect on chromatin accessibility (ChIP-Seq)

| PRJNA1081446 | ENA

The histone acetylation module and histone chaperone in the Arabidopsis NuB4 complex have synergistic effect on chromatin accessibility (ATAC-Seq)

Project description:The histone acetylation module and histone chaperone in the Arabidopsis NuB4 complex have synergistic effect on chromatin accessibility (ATAC-Seq)

| PRJNA1081447 | ENA

The histone acetylation module and histone chaperone in the Arabidopsis NuB4 complex have synergistic effect on chromatin accessibility

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

2024-10-25 | GSE259416 | GEO

Genome-wide maps of histone H2A.Z and its chaperone.

Project description:We use ChIP-Seq technology to profile the occupancy of histone H2A.Z and its chaperone in HeLa cells genome wide to check if they are co-colocalized. H2A.Z is ChIPed by antibody and its chaperone is tagged by Flag and ChIPed by M2 beads against Flag. ChIPed fragments are sequenced by Illumina HiSeq 2000 platform.

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The histone chaperone ANP32B regulates chromatin incorporation of the atypical human histone variant macroH2A

Project description:Eukaryotic chromatin structure is highly conserved, with the canonical histone proteins revealing only small sequence changes across species. Yet, all vertebrates exhibit three much larger histone H2A variants, macroH2A. A distinctive feature of these atypical histones is the globular macrodomain module, which can bind metabolites and is connected to the histone fold through a flexible linker. MacroH2A variants impact heterochromatin organization, transcription regulation and establish a barrier for cellular reprogramming. However, the mechanisms of how these large H2A variants are incorporated into chromatin and the identity of any chaperones required for histone deposition have remained elusive. Here, we developed a split-GFP-based cellular readout for histone incorporation and conducted a genome-wide mutagenesis screen in haploid human cells to identify proteins that regulate macroH2A dynamics. We identified and validated the histone chaperone ANP32B as a regulator of macroH2A chromatin deposition. ANP32B associates with macroH2A in cells and in vitro binds to histones with low nanomolar affinity. In vitro nucleosome assembly assays show that ANP32B stimulates deposition of macroH2A-H2B and not of H2A-H2B onto tetraso me. In cells, depletion of ANP32B in cells strongly affects global macroH2A deposition, revealing ANP32B as a macroH2A chaperone. Our study highlights the power of haploid cell functional genomics coupled with cellular imaging to identify factors that are required for chromatin plasticity and diversity.

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2021-04-14 | GSE154445 | GEO

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