Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage [ATAC-seq]

ABSTRACT: ATAC-seq from mouse ESC with stably integrated Zscan4c-GFP reporter.

ORGANISM(S): Mus musculus

PROVIDER: GSE140620 | GEO | 2020/03/22

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage.

Project description:Zinc finger protein Zscan4 is selectively expressed in mouse two-cell (2C) embryos undergoing zygotic genome activation (ZGA) and in a rare subpopulation of embryonic stem cells with 2C-like features. Here, we show that Zscan4 specifically recognizes a subset of (CA)n microsatellites, repeat sequences prone to genomic instability. Zscan4-associated microsatellite regions are characterized by low nuclease sensitivity and high histone occupancy. In vitro, Zscan4 binds nucleosomes and protects them from disassembly upon torsional strain. Furthermore, Zscan4 depletion leads to elevated DNA damage in 2C mouse embryos in a transcription-dependent manner. Together, our results identify Zscan4 as a DNA sequence-dependent microsatellite binding factor and suggest a developmentally regulated mechanism, which protects fragile genomic regions from DNA damage at a time of embryogenesis associated with high transcriptional burden and genomic stress.

| S-EPMC7083622 | biostudies-literature

Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage [RNA-seq]

Project description:2C-like cells or pluripotent cells were isolated from Zprom::GFP and Zprom::GFP-Zscan4 mouse ESC reporter lines to measure changes in gene expression.

2020-03-22 | GSE140615 | GEO

Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage [ChIP-seq]

Project description:Genome-wide binding analysis of Zscan4 showed sequence-specific occupancy at (CA)n microsatellite repeats in 2C-like cells. Genome-wide occupancy profiling of FACT subunit SSRP1 in curaxin-treated mouse ESC demonstrated re-localization from transcription start sites to Zscan4 binding sites.

2020-03-22 | GSE140619 | GEO

Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage

Project description:This SuperSeries is composed of the SubSeries listed below.

2020-03-22 | GSE140621 | GEO

Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage

Project description:Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage

| PRJNA590251 | ENA

Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage [ATAC-seq]

Project description:Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage [ATAC-seq]

| PRJNA590256 | ENA

Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage [ChIP-seq]

Project description:Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage [ChIP-seq]

| PRJNA590257 | ENA

Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage [RNA-seq]

Project description:Zscan4 binds nucleosomal microsatellite DNA and protects mouse two-cell embryos from DNA damage [RNA-seq]

| PRJNA590258 | ENA

The tardigrade damage suppressor protein binds to nucleosomes and protects DNA from hydroxyl radicals.

Project description:Tardigrades, also known as water bears, are animals that can survive extreme conditions. The tardigrade Ramazzottius varieornatus contains a unique nuclear protein termed Dsup, for damage suppressor, which can increase the resistance of human cells to DNA damage under conditions, such as ionizing radiation or hydrogen peroxide treatment, that generate hydroxyl radicals. Here we find that R. varieornatus Dsup is a nucleosome-binding protein that protects chromatin from hydroxyl radicals. Moreover, a Dsup ortholog from the tardigrade Hypsibius exemplaris similarly binds to nucleosomes and protects DNA from hydroxyl radicals. Strikingly, a conserved region in Dsup proteins exhibits sequence similarity to the nucleosome-binding domain of vertebrate HMGN proteins and is functionally important for nucleosome binding and hydroxyl radical protection. These findings suggest that Dsup promotes the survival of tardigrades under diverse conditions by a direct mechanism that involves binding to nucleosomes and protecting chromosomal DNA from hydroxyl radicals.

| S-EPMC6773438 | biostudies-literature

The Drosophila telomere-capping protein Verrocchio binds single-stranded DNA and protects telomeres from DNA damage response.

Project description:Drosophila telomeres are sequence-independent structures maintained by transposition to chromosome ends of three specialized retroelements rather than by telomerase activity. Fly telomeres are protected by the terminin complex that includes the HOAP, HipHop, Moi and Ver proteins. These are fast evolving, non-conserved proteins that localize and function exclusively at telomeres, protecting them from fusion events. We have previously suggested that terminin is the functional analogue of shelterin, the multi-protein complex that protects human telomeres. Here, we use electrophoretic mobility shift assay (EMSA) and atomic force microscopy (AFM) to show that Ver preferentially binds single-stranded DNA (ssDNA) with no sequence specificity. We also show that Moi and Ver form a complex in vivo. Although these two proteins are mutually dependent for their localization at telomeres, Moi neither binds ssDNA nor facilitates Ver binding to ssDNA. Consistent with these results, we found that Ver-depleted telomeres form RPA and ?H2AX foci, like the human telomeres lacking the ssDNA-binding POT1 protein. Collectively, our findings suggest that Drosophila telomeres possess a ssDNA overhang like the other eukaryotes, and that the terminin complex is architecturally and functionally similar to shelterin.

| S-EPMC5389638 | biostudies-literature

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