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Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation [H2AK9ac ChIP-seq]

ABSTRACT: Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation [H2AK9ac ChIP-seq]

PROVIDER: PRJNA683657 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR13221372.fastq.gz	Fastqsanger.gz
	SRR13221373.fastq.gz	Fastqsanger.gz
	SRR13221374.fastq.gz	Fastqsanger.gz
	SRR13221375.fastq.gz	Fastqsanger.gz
	SRR13221376.fastq.gz	Fastqsanger.gz

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Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation

Project description:Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation

| PRJNA683655 | ENA

Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation [RNA-seq]

Project description:Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation [RNA-seq]

| PRJNA683626 | ENA

Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation [ARID2 and PBRM1 ChIP-seq]

Project description:Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation [ARID2 and PBRM1 ChIP-seq]

| PRJNA803895 | ENA

Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation [RNA-seq]

Project description:Histone proteolysis is a poorly understood phenomena by which the N-terminal tail of histones are irreversible cleaved by intracellular proteases. During development histone PTMs are known orchestrate gene expression and ultimately cell fate decision, therefore it will be key to decipher underlying mechanisms that lead to proteolysis during cellular differentiation. Previous reports have found that histone H2A is cleaved at the C-terminus, and here we found that the N-terminal is also proteolytically clipped and removed by the lysosomal protease Cathepsin L. Using quantitative mass spectrometry (MS), we identified L23 to be the primary site for this protease, with this clipped H2A (cH2A) form representing ~1% of the total H2A reaching a maximum after 4 days of differentiation. Using Chip-seq, we found reduced proteolysis, lead to increase acetylated H2A at promoter regions in differentiated ES cells. We also report novel readers of acetylated H2A during in pluripotency as we identified members of the pBAF complex to recognize different forms of H2A acetylation. Moreover, our data showed that this recognition is abolished upon proteolysis. All in, our data suggest that proteolysis serve as a quick mechanism to silence genes involve in pluripotency and destabilize the nucleosome core particle as indicated by protein degradation studies.

2021-12-31 | GSE162877 | GEO

Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation [H2AK9ac ChIP-seq]

2021-12-31 | GSE162874 | GEO

Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation [ARID2 and PBRM1 ChIP-seq]

2022-03-22 | GSE196205 | GEO

Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation

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

2021-12-31 | GSE162896 | GEO

Centromeric DNA destabilizes H3 nucleosomes to promote CENP-A deposition during the cell cycle

Project description:Centromeric DNA destabilizes H3 nucleosomes to promote CENP-A deposition during the cell cycle

| PRJNA417043 | ENA

Effect of DNA binding small molecules on the genomic distribution of nucleosomes with H3K27Ac

Project description:Small molecule CBL0137 destabilizes nucleosome directly via binding to DNA. Effect of CBL0137 on nucleosomes with mark specific for more open chromatin characteristic for promoters and enhancers versus all nucleosomes H3 was measured.

2018-07-20 | GSE117409 | GEO

Glutamine methylation on Histone H2A is an RNA Polymerase I dedicated modification

Project description:Nucleosomes are decorated with numerous post-translational modifications capable of influencing many DNA processes. Here, we describe a new class of modification, methylation of glutamine, occurring on yeast histone H2A at position 105 (Q105) and human H2A at Q104. We identify Nop1 as the methyltransferase in yeast and we demonstrate that Fibrillarin is the equivalent enzyme in human cells. Glutamine methylation of H2A is restricted to the nucleolus. Global analysis in yeast, using a H2AQ105me specific antibody, show that this modification is exclusively enriched over the 35S rDNA transcriptional unit. We show that the Q105 residue is part of the binding site for the histone chaperone FACT (Facilitator of Transcription) complex. Methylation of Q105 or its substitution to alanine disrupts binding to FACT in vitro. A yeast strain mutated at Q105 exhibits a defect in histone incorporation and shows increased transcription at rDNA genes. This defect is phenocopied by mutations in FACT that decrease its activity. Together these data identify glutamine methylation of H2A as the first histone epigenetic mark dedicated to a specific RNA polymerase and define its function as a regulator of FACT interaction with nucleosomes.

2014-01-21 | E-MTAB-1447 | biostudies-arrayexpress

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