Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7. [ChIRP-seq]

ABSTRACT: The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7. [ChIRP-seq]

PROVIDER: PRJNA730846 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR14577534.fastq.gz	Fastqsanger.gz
	SRR14577535.fastq.gz	Fastqsanger.gz
	SRR14577536.fastq.gz	Fastqsanger.gz
	SRR14577537.fastq.gz	Fastqsanger.gz
	SRR16506413.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 17

Similar Datasets

The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7. [ChIRP-seq]

Project description:The histone acetyltransferase p300 (also known as KAT3B) is a general transcriptional coactivator that introduces the H3K27ac mark on enhancers triggering their activation and gene transcription. Genome-wide screenings demonstrated that a large fraction of long non-coding RNAs (lncRNAs) plays a role in cellular processes and organ development although the underlying molecular mechanisms remain largely unclear. We found 122 lncRNAs that interacts directly with p300. In depth analysis of one of these, lncSmad7, is required to maintain ESC self-renewal and it interacts to the C-terminal domain of p300. lncSmad7 also contains predicted RNA-DNA Hoogsteen forming base pairing. Combined Chromatin Isolation by RNA precipitation followed by sequencing (ChIRP-seq) together with CRISPR/Cas9 mutagenesis of the target sites demonstrate that lncSmad7 binds and recruits p300 to enhancers in trans, to trigger enhancer acetylation and transcriptional activation of its target genes. Thus, these results unveil a new mechanism by which p300 is recruited to the genome.

2022-02-10 | GSE174636 | GEO

The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7. [RNA-Seq]

2022-02-10 | GSE154737 | GEO

The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7. [PAR-CLIP]

2022-02-10 | GSE154732 | GEO

The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7. [ChIP-seq]

2022-02-10 | GSE154731 | GEO

The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7

Project description:The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7

| PRJNA647348 | ENA

The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7. [PAR-CLIP]

Project description:The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7. [PAR-CLIP]

| PRJNA647358 | ENA

The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7. [RNA-Seq]

Project description:The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7. [RNA-Seq]

| PRJNA647360 | ENA

The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7. [ChIP-seq]

Project description:The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7. [ChIP-seq]

| PRJNA647357 | ENA

The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7.

Project description:The histone acetyltransferase p300 (also known as KAT3B) is a general transcriptional coactivator that introduces the H3K27ac mark on enhancers triggering their activation and gene transcription. Genome-wide screenings demonstrated that a large fraction of long non-coding RNAs (lncRNAs) plays a role in cellular processes and organ development although the underlying molecular mechanisms remain largely unclear (1,2). We found 122 lncRNAs that interacts directly with p300. In depth analysis of one of these, lncSmad7, is required to maintain ESC self-renewal and it interacts to the C-terminal domain of p300. lncSmad7 also contains predicted RNA-DNA Hoogsteen forming base pairing. Combined Chromatin Isolation by RNA precipitation followed by sequencing (ChIRP-seq) together with CRISPR/Cas9 mutagenesis of the target sites demonstrate that lncSmad7 binds and recruits p300 to enhancers in trans, to trigger enhancer acetylation and transcriptional activation of its target genes. Thus, these results unveil a new mechanism by which p300 is recruited to the genome.

| S-EPMC8934626 | biostudies-literature

Regulation of p300 acetyltransferase activity by the TAZ2 domain [ATAC-seq]

Project description:The E1A binding protein P300 (EP300, also known as p300, lysine acetyltransferase 3B or KAT3B) and its close paralogue CREB-binding protein (CREBBP, aka CBP or KAT3A) possess intrinsic histone acetyltransferase (HAT) activity that can act on both histone and non-histone proteins. P300 and CBP are composed of multiple conserved protein domains, many of which are in proximity to the HAT domain modulating its catalytic activity. Here we show that the TAZ2 domain regulates the intrinsic catalytic activity of p300 in vitro and histone acetylation and chromatin accessibility in cells. Our study extends the knowledge of p300 self-regulation and provides new therapeutic stratagies for human cancers with corresponding p300/CBP mutations.

2023-08-07 | GSE193647 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data