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Acetylation of histone H3K27 signals the transcriptional elongation for estrogen receptor alpha

ABSTRACT: Acetylation of histone H3K27 signals the transcriptional elongation for estrogen receptor alpha

PROVIDER: PRJNA602595 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR10948655.fastq.gz	Fastqsanger.gz
	SRR10948656.fastq.gz	Fastqsanger.gz
	SRR10948657.fastq.gz	Fastqsanger.gz

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Similar Datasets

Acetylation of histone H3K27 signals the transcriptional elongation for estrogen receptor alpha

Project description:As approximately 70% of human breast tumors are estrogen receptor α (ERα)-positive, estrogen and ERα play essential roles in breast cancer development. By interrupting the ERα signaling pathway, endocrine therapy has been proven to be an effective therapeutic strategy. In the present study, we identified a novel mechanism by which Transcription Start Site (TSS)-associated histone H3K27 acetylation signals the Super Elongation Complex (SEC) to regulate transcriptional elongation of the ERα gene. The SEC interacts with H3K27ac on ERα TSS through its scaffold protein AFF4. Depletion of AFF4 by siRNA or CRISPR/Cas9 dramatically reduces expression of ERα and its target genes, consequently inhibiting breast cancer cell growth. More importantly, AFF4 mutant which lacks H3K27ac interaction failed to rescue ERα gene expression, suggesting H3K27 acetylation at TSS region is a key mark bridging the transition from transcriptional initiation to elongation, and perturbing SEC function can be an alternative strategy for targeting ERα signaling pathway at the level of chromatin.

2020-01-31 | GSE144036 | GEO

Acetylation of histone H3K27 signals the transcriptional elongation for estrogen receptor alpha.

Project description:As approximately 70% of human breast tumors are estrogen receptor α (ERα)-positive, estrogen and ERα play essential roles in breast cancer development. By interrupting the ERα signaling pathway, endocrine therapy has been proven to be an effective therapeutic strategy. In this study, we identified a mechanism by which Transcription Start Site (TSS)-associated histone H3K27 acetylation signals the Super Elongation Complex (SEC) to regulate transcriptional elongation of the ESR1 (ERα) gene. SEC interacts with H3K27ac on ESR1 TSS through its scaffold protein AFF4. Depletion of AFF4 by siRNA or CRISPR/Cas9 dramatically reduces expression of ESR1 and its target genes, consequently inhibiting breast cancer cell growth. More importantly, a AFF4 mutant which lacks H3K27ac interaction failed to rescue ESR1 gene expression, suggesting H3K27 acetylation at TSS region is a key mark bridging the transition from transcriptional initiation to elongation, and perturbing SEC function can be an alternative strategy for targeting ERα signaling pathway at chromatin level.

| S-EPMC7138820 | biostudies-literature

CBP/P300 Dependent Histone H3K27 Acetylation

Project description:Enhancer Activity Requires CBP/P300 Bromodomain Dependent Histone H3K27 Acetylation

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H3K27 acetylation and gene expression during late spermatogenesis

Project description:H3K27 acetylation and gene expression during late spermatogenesis

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H3K27 acetylation and gene expression during late spermatogenesis

Project description:ChIP-seq for H3K27 acetylation and RNA-seq were performed during spermatogenesis. We analyzed two representative stages of spermatogenesis: purified pachytene spermatocytes (PS) undergoing meiosis; and postmeiotic round spermatids (RS) from adult testes.

2018-02-05 | GSE107398 | GEO

Impaired Liver X Receptor alpha phosphorylation affects hepatic chromatin H3K27 acetylation patterns

Project description:Impaired Liver X Receptor alpha phosphorylation affects hepatic chromatin H3K27 acetylation patterns

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H3K27 acetylation profiling of B cells from Mb1Cre and Mct1f/fMb1Cre mice

Project description:Using ChIP-seq we identified H3K27 acetylation loci in B cells from Mb1Cre and Mct1f/fMb1Cre mice

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H3K27 Acetylation profile of hypothyroid NCoR1KO mice

Project description:We ablated the expression of the Nuclear Receptor Corepressor 1 specifically in mice livers and rendered them hypothyroid. Then we performed H3K27 acetylation CHIP-Seq. We found decreased H3K27ac in the livers of hypothyroid wild type and NCoR1KO mice. Therefore, we concluded that the thyroid hormone receptor may recruit histone deacetilases independently of NCoR1.

2017-09-18 | GSE99475 | GEO

Cytosolic acetyl-CoA promotes histone acetylation predominantly at H3K27 in Arabidopsis

Project description:Acetyl-Coenzyme A (acetyl-CoA) is a central metabolite and the acetyl source for protein acetylation, particularly histone acetylation that promotes gene expression. However, the effect of acetyl-CoA levels on histone acetylation status in plants remains unknown. Here, we show that malfunctioned cytosolic acetyl-CoA carboxylase1 (ACC1) in Arabidopsis leads to elevated levels of acetyl-CoA and promotes histone hyperacetylation predominantly at lysine 27 of histone H3 (H3K27). The increase of H3K27 acetylation (H3K27ac) is dependent on ATP-citrate lyase which cleaves citrate to acetyl-CoA in the cytoplasm, and requires histone acetyltransferase GCN5. A comprehensive analysis of the transcriptome and metabolome in combination with the genome-wide H3K27ac profiles of acc1 mutants, demonstrate the dynamic changes of H3K27ac, gene transcripts and metabolites occurring in the cell by the increased levels of acetyl-CoA. This study suggests that H3K27ac is an important link between cytosolic acetyl-CoA level and gene expression in response to the dynamic metabolic environments in plants.

2017-09-25 | GSE79524 | GEO

Genome-wide profiling of H3K9/K14 Acetylation and H3K27 trimethylation at promoters in the human lung embryonic fibroblast cell line MRC5

Project description:Genome-wide profiling of H3K9/K14 Acetylation and H3K27 trimethylation at promoters in the human lung embryonic fibroblast cell line MRC5

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