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Differential contribution of p300 and CBP to regulatory elements in mESCs [ATAC-seq]

ABSTRACT: Differential contribution of p300 and CBP to regulatory elements in mESCs [ATAC-seq]

PROVIDER: PRJNA577736 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR10288447_1.fastq.gz	Fastqsanger.gz
	SRR10288447_2.fastq.gz	Fastqsanger.gz
	SRR10288448_1.fastq.gz	Fastqsanger.gz
	SRR10288448_2.fastq.gz	Fastqsanger.gz
	SRR10288449_1.fastq.gz	Fastqsanger.gz

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Differential contribution of p300 and CBP to regulatory elements in mESCs

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Differential contribution of p300 and CBP to regulatory elements in mESCs

Project description:In this study we analyze the individual contribution of p300 and CBP to the H3K27ac landscape, chromatin accessibility, and transcription in mESC. This SuperSeries is composed of the SubSeries listed below.

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Differential contribution of p300 and CBP to regulatory elements in mESCs [ChIP-seq]

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Differential contribution of p300 and CBP to regulatory elements in mESCs [RNA-seq]

Project description:Differential contribution of p300 and CBP to regulatory elements in mESCs [RNA-seq]

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Differential contribution of p300 and CBP to regulatory elements in mESCs [RNA-seq]

Project description:In this study we analyze the individual contribution of p300 and CBP to the H3K27ac landscape, chromatin accessibility, and transcription in mESC.

2020-07-16 | GSE138924 | GEO

Differential contribution of p300 and CBP to regulatory elements in mESCs [ATAC-seq]

Project description:In this study we analyze the individual contribution of p300 and CBP to the H3K27ac landscape, chromatin accessibility, and transcription in mESC.

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Differential contribution of p300 and CBP to regulatory elements in mESCs [ChIP-seq]

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CBP/p300 transcriptome

Project description:CBP/p300 transcriptome

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P300-CBP

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Epigenetic mechanisms to propagate histone acetylation by p300/CBP

Project description:Histone acetylation is important for the activation of gene transcription but little is known about its direct ‘read/write’ mechanisms. Here, we report cryo-electron microscopy structures in which a p300/CBP multidomain monomer recognizes histone H4 N-terminal tail (NT) acetylation (ac) in a nucleosome and acetylates non-H4 histone NTs within the same nucleosome. p300/CBP not only recognized H4NTac via the bromodomain pocket responsible for ‘reading’, but also interacted with the DNA minor grooves via the outside of that pocket. This directed the catalytic center of p300/CBP to one of the non-H4 histone NTs. The primary target that p300 ‘writes’ by ‘reading’ H4NTac was H2BNT, and H2BNTac promoted H2A-H2B dissociation from the nucleosome. We propose a model in which p300/CBP ‘replicates’ histone NT acetylation within the H3-H4 tetramer to inherit epigenetic storage, and ‘transcribes’ it from the H3-H4 tetramer to the H2B-H2A dimers to activate context-dependent gene transcription through local nucleosome destabilization.

2023-05-08 | PXD040835 | Pride

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