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Intergenerationally maintained Histone H4 lysine 16 acetylation is instructive for future gene activation

ABSTRACT: Intergenerationally maintained Histone H4 lysine 16 acetylation is instructive for future gene activation

PROVIDER: PRJNA535511 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11409500_1.fastq.gz	Fastqsanger.gz
	SRR11409500_2.fastq.gz	Fastqsanger.gz
	SRR11409501_1.fastq.gz	Fastqsanger.gz
	SRR11409501_2.fastq.gz	Fastqsanger.gz
	SRR11409502_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

Intergenerationally maintained Histone H4 lysine 16 acetylation is instructive for future gene activation

Project description:Before zygotic genome activation (ZGA) the quiescent genome undergoes reprogramming to transition into the transcriptionally active state. However, the mechanisms underlying euchromatin establishment during early embryogenesis remain poorly understood. Here, we show that histone H4 lysine-16 acetylation (H4K16ac) is maintained from oocytes to fertilized embryos in Drosophila and mammals. H4K16ac forms large domains that control nucleosome accessibility of promoters prior to ZGA in flies. Maternal depletion of MOF acetyl-transferase leading to H4K16ac loss causes aberrant Pol II recruitment, compromises the 3D organization of the active genomic compartments during ZGA and consequently causes downregulation of post-zygotically expressed genes. Germline depletion of histone deacetylases revealed that other acetyl marks cannot compensate for H4K16ac loss in the oocyte. Moreover, zygotic re-expression of MOF was neither able to restore embryonic viability nor onset of X chromosome dosage compensation. Thus, maternal H4K16ac provides an instructive function to the offspring, priming future gene activation.

2020-06-04 | GSE130335 | GEO

Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics

Project description:Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics

| PRJNA545040 | ENA

Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics

Project description:Chromatin is decorated with diverse histone posttranslational modifications (PTMs) that are involved in regulating chromatin structure and dynamics during various DNA-associated processes such as gene transcription, DNA replication and DNA damage repair. Here, we combine a chemical reporter with mass spectrometry to identify a new class of histone PTM, lysine glutarylation (Kglu), occurring at 27 lysine residues on human core histones. The characterization of an evolutionarily conserved Kglu mark at histone H4 lysine 91 (H4K91glu) using a semisynthetic glutarylated protein reveals that this negatively charged modification greatly destabilizes nucleosome by weakening the interactions between histone H2A/H2B dimers and H3/H4 tetramer in vitro. The replacement of H4K91 by glutamic acid in S. cerevisiae to mimic glutarylation influences chromatin structure and thereby results in a global up-regulation of transcription and defects in cell cycle progression, DNA damage repair and telomere silencing in vivo. In mammalian cells, H4K91glu is mainly enriched at promoter regions of highly expressed genes. A down-regulation of H4K91glu is tightly associated with chromatin condensation during mitosis and in response to DNA damage. The cellular dynamics of H4K91glu is controlled by Sirt7 as a deglutarylase and KAT2A as a glutaryltransferase. This study designates a new histone mark (Kglu) as a new regulatory mechanism for chromatin dynamics.

2019-09-16 | GSE131807 | GEO

Mapping of H4-acetylated chromatin modifications in differentiating human primary myoblasts

Project description:We assessed the genomic distribution of H4-acetylated chromatin by ChIP using SNP chips and an antibody specific to four acetylated lysine residues of H4. Keywords: Comparative genomic hybridization

2006-08-28 | GSE4132 | GEO

Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes (ChIP-seq)

Project description:To study the role of Histone H4 lysine 20 mono- and tri-methylation (H4K20me1, H4K20me3) in relationship to chromatin accessibility and gene expression, we report the application of high-throughput profiling of these marks in Human Osteosarcoma U2OS and Mouse Fibroblast (MEF) cells with Set8 knockdown or control siRNA treatment. We find that H4K20me1 contributes to the open chromatin structure at active genes.

2021-06-04 | GSE156216 | GEO

Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes (ATAC-seq_DRB)

Project description:To study the role of Histone H4 lysine 20 mono- and tri-methylation (H4K20me1, H4K20me3) in relationship to chromatin accessibility and gene expression, we report the application of high-throughput profiling of these marks in synchronized and asynchronous Human Osteosarcoma U2OS and asynchronous Mouse Fibroblast (MEF) cells with Set8 knockdown or control siRNA treatment. We find that H4K20me1 contributes to the open chromatin structure at active genes.

2021-06-04 | GSE173313 | GEO

Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes (ATAC-seq)

Project description:To study the role of Histone H4 lysine 20 mono- and tri-methylation (H4K20me1, H4K20me3) in relationship to chromatin accessibility and gene expression, we report the application of high-throughput profiling of these marks in synchronized and asynchronous Human Osteosarcoma U2OS and asynchronous Mouse Fibroblast (MEF) cells with Set8 knockdown or control siRNA treatment. We find that H4K20me1 contributes to the open chromatin structure at active genes.

2021-06-04 | GSE156215 | GEO

Transcriptomic analysis of the effect of histone H4 K31R mutation in U2OS cells

Project description:To explore the genome-wide gene expression changes induced by the K31R mutation in the histone H4 protein, we performed RNA-sequencing analysis in U2OS cells expressing either wildtype H4 or K31R mutant H4. We found that the lysine (K) to arginine (R) mutation mainly affected oxidative phosphorylation, mtiochondria dysfunction and et al, but not DNA damage signaling pathways.

2019-02-20 | GSE126451 | GEO

Dynamic competing histone H4 K5K8 acetylation and butyrylation are hallmarks of highly active gene promoters

Project description:Newly discovered histone lysine acylations increase the functional diversity of nucleosomes well beyond acetylation. Here, we focus on histone butyrylation in the context of sperm cell differentiation. Specifically, we investigate the butyrylation of histone H4 lysine 5 and 8 at gene promoters, where acetylation guides the binding of Brdt, a bromodomain-and-extra-terminal protein, thereby mediating stage-specific gene expression programs. Genome-wide mapping data show that highly active Brdt-bound gene promoters systematically harbour competing histone acetylation and butyrylation marks at H4 K5 and K8. Histone butyrylation, despite acting as a direct stimulator of transcription, competes with acetylation, especially at H4 K5, to prevent Brdt binding. The observed in vivo H4 K5K8 acetylation butyrylation state at active promoters is reproduced in vitro where p300 indistinctly acetylates and butyrylates H4 K5 and K8. Altogether, highly active gene promoter regions are characterized by alternating H4 acetylation and butyrylation sustaining direct gene activation and a dynamic bromodomain binding.

2016-07-13 | GSE77277 | GEO

Acetylation of histone H4 at lysine 44 facilitates meiotic recombination by creating accessible chromatin [Mnase-seq]

Project description:Meiotic recombination hotspots are associated with histone post-translational modifications and open chromatin. However, it remains unclear how histone modifications and chromatin structure directly regulate meiotic recombination. Here, we identify acetylation of histone H4 at Lys44 (H4K44ac) as a new histone modification, occurring on the nucleosomal lateral surface. We show that H4K44ac is specific to yeast sporulation, rising during yeast meiosis and displaying genome-wide enrichment at recombination hotspots in meiosis. The H4K44 residue is required for normal meiotic recombination, for normal levels of double strand breaks during meiosis, and for optimal sporulation. Non-modifiable substitution H4K44R results in reduced MNase digestion and decreased binding of recombination-associated proteins at hotspots. Our results show that H4K44ac creates an accessible chromatin environment for key proteins to facilitate meiotic recombination. Two samples, one WT MNase-seq and one MNase-seq from yeast with a lysine->arginine mutation at H4K44, no replicates Two replicates each of MNase-seq in WT and H4K44->R mutant yeast grown in YPD or YPA.

2015-12-07 | E-GEOD-59004 | biostudies-arrayexpress

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