Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

STAG proteins mediate heterochromatin organization to support translation and cell identity [RNA-Seq]

ABSTRACT: STAG proteins mediate heterochromatin organization to support translation and cell identity [RNA-Seq]

PROVIDER: PRJNA671631 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR12888165_1.fastq.gz	Fastqsanger.gz
	SRR12888165_2.fastq.gz	Fastqsanger.gz
	SRR12888166_1.fastq.gz	Fastqsanger.gz
	SRR12888166_2.fastq.gz	Fastqsanger.gz
	SRR12888167_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 36

Similar Datasets

STAG proteins mediate heterochromatin organization to support translation and cell identity [UMI-4C]

Project description:STAG proteins mediate heterochromatin organization to support translation and cell identity [UMI-4C]

| PRJNA671632 | ENA

STAG proteins mediate heterochromatin organization to support translation and cell identity [Iso-Seq]

Project description:STAG proteins mediate heterochromatin organization to support translation and cell identity [Iso-Seq]

| PRJNA673168 | ENA

STAG proteins mediate heterochromatin organization to support translation and cell identity [Iso-Seq]

Project description:Abstract to add later

2021-06-06 | GSE160387 | GEO

STAG proteins mediate heterochromatin organization to support translation and cell identity [UMI-4C]

Project description:Abstract to be added later

2021-06-06 | GSE160015 | GEO

STAG proteins mediate heterochromatin organization to support translation and cell identity [RNA-Seq]

Project description:Abstract to be added later

2021-06-06 | GSE160014 | GEO

Complete loss of H3K9 methylation dissolves mouse heterochromatin organization

Project description:Histone H3 lysine 9 (H3K9) methylation is a central epigenetic modification that defines heterochromatin from unicellular to multicellular organisms. In mammalian cells, H3K9 methylation can be catalyzed by at least six distinct SET domain enzymes: Suv39h1/Suv39h2, Eset1/Eset2 and G9a/Glp. We used mouse embryonic fibroblasts (MEFs) with a conditional mutation for Eset1 and introduced progressive deletions for the other SET domain genes by CRISPR/Cas9 technology. Compound mutant MEFs for all 6 SET domain methyltransferase (KMT) genes lack all H3K9 methylation states, derepress nearly all families of repeat elements and display genomic instabilities. Strikingly, the 6KO H3K9 KMT MEFs no longer maintain heterochromatin organization and have lost electron-dense heterochromatin. This is the first analysis of H3K9 methylation deficient mammalian chromatin and reveals a crucial function for H3K9 methylation in protecting heterochromatin organization and genome integrity.

2021-05-27 | PXD018175 | Pride

Single-cell RNA sequencing (scRNA-seq) on Treg cells from PBS and STAg treated mice

Project description:To identify cell composition and characterize transcriptional regulation in regulatory T (Treg) cells derived from mice subjected to soluble tachyzoite antigen (STAg) of Toxoplasma gondii treatment, we prepared splenic CD4+CD25+ Treg cells from PBS and STAg treated mice, and performed scRNA-seq using the 10× Genomics method.

2020-12-31 | GSE132803 | GEO

Drosophila HP1a IP-MS - The composition and organization of Drosophila heterochromatin are heterogeneous and dynamic

Project description:Heterochromatin is enriched for characteristic epigenetic factors, including Heterochromatin Protein 1a (HP1a) and is essential for many organismal functions. However, how this nuclear domain is organized and functions is unclear. We extensively investigated heterochromatin protein compostion by biochemically purifying Drosophila melanogaster HP1a interactors.

2016-08-18 | PXD003780 | Pride

MeCP2 heterochromatin organization is modulated by arginine methylation and serine phosphorylation

Project description:Rett syndrome is a human intellectual disability disorder that is associated with mutations in the X-linked MECP2 gene. Theepigenetic reader MeCP2 binds to methylated cytosines on the DNA and regulates chromatin organization. We have shownpreviously that MECP2 Rett syndrome missense mutations are impaired in chromatin binding and heterochromatinreorganization. Here, we performed a proteomics analysis of post-translational modifications of MeCP2 isolated from adult mousebrain. We show that MeCP2 carries various post-translational modifications, among them phosphorylation on S80 and S421, whichlead to minor changes in either heterochromatin binding kinetics or clustering. We found that MeCP2 is (di)methylated on severalarginines and that this modification alters heterochromatin organization. Interestingly, we identified the Rett syndrome mutationsite R106 as a dimethylation site. In addition, co-expression of protein arginine methyltransferases 1 and 6 lead to a decrease ofheterochromatin clustering. Altogether, we identified and validated novel modifications of MeCP2 in the brain and show that thesecan modulate its ability to bind as well as reorganize heterochromatin, which may play a role in the pathology of Rett syndrome.

2022-10-15 | PXD033696 | Pride

Forced expression of MSR repeat transcripts breaks heterochromatin organization

Project description:Mouse heterochromatin is characterized by transcriptionally competent major satellite repeat (MSR) sequences and it has been proposed that MSR repeat RNA contributes to the integrity of heterochromatin. We established an inducible dCas9-effector system in mouse embryonic fibroblasts, where we can target dCas9-VPR (transcriptional activator) and dCas9-KM (transcriptional repressor) to MSR repeat sequences. We show that induction of dCas9-VPR forces significant MSR RNA output, while induction of dCas9-KM silences MSR transcription. Both approaches perturb heterochromatin organization, where the dCas9-VPR leads to an immediate dispersion of heterochromatin and dCas9-KM induction results in a delayed aggregation of heterochromatin. MEF cells with the forced expression of MSR RNA are not viable and the defects in heterochromatin organization cannot be reverted. This study highlights the importance of restricting MSR RNA output to maintain heterochromatin integrity and also reveals that the structural organization of heterochromatin is governed by the transcriptional state of the underlying MSR repeats.

2025-03-23 | GSE262294 | 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