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The EZH2-PRC2-H3K27me3 axis governing the endometrial cell cycle and differentiation for successful blastocyst invasion

ABSTRACT: The EZH2-PRC2-H3K27me3 axis governing the endometrial cell cycle and differentiation for successful blastocyst invasion

PROVIDER: PRJNA854933 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR19925013_1.fastq.gz	Fastqsanger.gz
	SRR19925013_2.fastq.gz	Fastqsanger.gz
	SRR19925014_1.fastq.gz	Fastqsanger.gz
	SRR19925014_2.fastq.gz	Fastqsanger.gz
	SRR19925015_1.fastq.gz	Fastqsanger.gz

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The EZH2-PRC2-H3K27me3 axis governing the endometrial cell cycle and differentiation for successful blastocyst invasion

Project description:Ezh2-catalyzing H3K27 trimethylation regulates uterine epithelial and stromal differentiation and blastocyst invasion, contributing to successful pregnancy outcomes.

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PRC2

Project description:PRC2

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PRC2 engages a bivalent H3K27M-H3K27me3 dinucleosome inhibitor.

Project description:A lysine-to-methionine mutation at lysine 27 of histone 3 (H3K27M) has been shown to promote oncogenesis in a subset of pediatric gliomas. While there is evidence that this "oncohistone" mutation acts by inhibiting the histone methyltransferase PRC2, the details of this proposed mechanism nevertheless continue to be debated. Recent evidence suggests that PRC2 must simultaneously bind both H3K27M and H3K27me3 to experience competitive inhibition of its methyltransferase activity. In this work, we used PRC2 inhibitor treatments in a transgenic H3K27M cell line to validate this dependence in a cellular context. We further used designer chromatin inhibitors to probe the geometric constraints of PRC2 engagement of H3K27M and H3K27me3 in a biochemical setting. We found that PRC2 binds to a bivalent inhibitor unit consisting of an H3K27M and an H3K27me3 nucleosome and exhibits a distance dependence in its affinity for such an inhibitor, which favors closer proximity of the 2 nucleosomes within a chromatin array. Together, our data precisely delineate fundamental aspects of the H3K27M inhibitor and support a model wherein PRC2 becomes trapped at H3K27M-H3K27me3 boundaries.

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Comparative trascriptomic analysis between early-blastocyst and Hatched blastocyst

Project description:Comparative trascriptomic analysis between porcine early-blastocyst and Hatched blastocyst collected around day 5-6 direct comparison with dye-swap; two different arrays with 6 Samples each

2015-06-21 | E-GEOD-38882 | biostudies-arrayexpress

Comparative trascriptomic analysis between early-blastocyst and Hatched blastocyst

Project description:Comparative trascriptomic analysis between porcine early-blastocyst and Hatched blastocyst collected around day 5-6

2015-06-21 | GSE38882 | GEO

Deletion of RING1A/B and loss of H2AK119ub1 affects PRC2 occupancy and H3K27me3 genome-wide

Project description:The chromatin modifying activities inherent to polycomb repressive complexes PRC1 and PRC2 play an essential role in gene regulation, cellular differentiation, and development. However, the mechanisms by which these complexes recognize their target sites and function together to form repressive chromatin domains remain poorly understood. Recruitment of PRC1 to target sites has been proposed to occur through a hierarchical process, dependent on the prior nucleation of PRC2 and placement of H3K27me3. Here, using a de novo targeting assay in mouse embryonic stem cells we unexpectedly discover that PRC1-dependent H2AK119ub1 leads to the recruitment of PRC2 and H3K27me3 to effectively initiate a polycomb domain. Genetic ablation of catalytic subunit of the PRC1 complex (RINGA/B) and ChIP-seq analysis of PRC1 and PRC2 components confirmed genome-wide decreases in PRC2 occupancy and H3K27me3 levels at PRC target sites. This activity is restricted to variant PRC1 complexes and genetic ablation experiments reveal that targeting of the variant PCGF1/PRC1 complex by KDM2B to CpG islands is required for polycomb domain formation and normal development. Together these observations provide a surprising new PRC1-dependent logic for PRC2 occupancy and polycomb domain formation. RING1A-/-;RING1Bfl/fl ES cells were treated with 800M-BM-5M tamoxifen for 48hours and compared to untreated control cells by ChIP-seq for RING1B, SUZ12, EZH2 and H3K27me3.

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C10ORF12 modulates PRC2 histone methyltransferase activity and H3K27me3 levels.

Project description:The polycomb repressive complex 2 (PRC2) catalyzes the methylation of histone H3 on lysine 27 (H3K27) to generate trimethyl-H3K27 (H3K27me3) marks, thereby leading to a repressive chromatin state that inhibits gene expression. C10ORF12 was recently identified as a novel PRC2 interactor. Here, we show that C10ORF12 specifically interacts with PRC2 through its middle region (positions 619-718). C10ORF12 significantly enhances the histone methyltransferase activity of PRC2 in vitro and dramatically increases the total H3K27me3 levels in HeLa cells. C10ORF12 also antagonizes Jarid2, which is an auxiliary factor of the PRC2.2 subcomplex, to promote increased H3K27me3 levels in HeLa cells. Moreover, C10ORF12 alters the substrate preference of PRC2. These results indicate that C10ORF12 functions as a positive regulator of PRC2 and facilitates PRC2-mediated H3K27me3 modification of chromatin. These findings provide new insight into the roles of C10ORF12 in regulating the activity of the PRC2 complex.

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Interplay between Nsd1 and PRC2 demarcates regions of H3K27me2 and H3K27me3

Project description:The core Polycomb Repressor Complex 2 (PRC2) is composed of Ezh1/2, Suz12, Eed and is responsible for mediating both H3K27me2 and H3K27me3. However, the mechanisms by which PRC2 demarcates these two repressive modifications in the genome are unknown. In a functional screen, we identified the H3K36 dimethyltransferase Nsd1 as a modulator of PRC2-mediated di- and trimethylation of H3K27. ChIP-Seq analysis following the depletion of Nsd1 revealed a global reduction in H3K36me2 and an increase in H3K27me3 at sites previously marked by H3K27me2. We show that the H3K36me2 at H3K27me2 marks co-occupy regions and provide evidence that the presence of H3K36me2 functions to restrict the spatial distribution of Polycomb mediated H3K27me3 domains.

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Interplay between Nsd1 and PRC2 demarcates regions of H3K27me2 and H3K27me3.

2018-03-29 | GSE107773 | GEO