Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Canine DUXC isoforms and functional similarity to human DUX4 [RNA-seq]

ABSTRACT: Canine DUXC isoforms and functional similarity to human DUX4 [RNA-seq]

PROVIDER: PRJNA780789 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR16955246.fastq.gz	Fastqsanger.gz
	SRR16955248.fastq.gz	Fastqsanger.gz
	SRR16955249.fastq.gz	Fastqsanger.gz
	SRR16955251.fastq.gz	Fastqsanger.gz
	SRR16955252.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 12

Similar Datasets

Canine DUXC isoforms and functional similarity to human DUX4

Project description:Canine DUXC isoforms and functional similarity to human DUX4

| PRJNA780786 | ENA

Canine DUXC isoforms and functional similarity to human DUX4 [ChIP-seq]

Project description:Canine DUXC isoforms and functional similarity to human DUX4 [ChIP-seq]

| PRJNA780790 | ENA

Canine DUXC isoforms and functional similarity to human DUX4 [RNA-seq]

Project description:Human DUX4 and mouse Dux transcription factors are normally expressed in the germ line and early embryonic cells where they activate the cleavage stage genes. The misexpression of DUX4 in skeletal muscles causes Facioscapulohumeral dystrophy (FSHD). In primates and rodents, DUX4 and Dux arose from retrotransposition of the mRNA from the ancestral intron-containing DUXC, which is not found in these species, and whether it has similar roles in the cleavage stage and FSHD as DUX4 and Dux are unknown. Here, we identified two isoforms of DUXC in canine testis tissues: One encodes the canonical double homeodomain (DUXC) similar to DUX4/Dux, and one contains an extra exon that disrupts the conserved amino-acid sequence of the first homeodomain (DUXC-ALT). We expressed DUXC and DUXC-ALT in canine skeletal muscle and found that the expression of DUXC induced retrotransposons and pluripotent programs similar to DUX4 and Dux, whereas DUXC-ALT did not robustly activate genes in these assays.

2021-12-03 | GSE188927 | GEO

Canine DUXC isoforms and functional similarity to human DUX4 [ChIP-seq]

2021-12-03 | GSE188926 | GEO

Canine DUXC isoforms and functional similarity to human DUX4

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

2021-12-03 | GSE188928 | GEO

Canine subcellular Proteomics

Project description:To facilitate canine proteomics research, we have generated a non-redundant canine protein sequence database, with entry name annotation based on sequence similarity to the human proteome. To evaluate the sequence-based annotation transfer, we performed a shotgun proteomics experiment on subcellular fractions of canine spleen.

2022-03-02 | PXD003847 | Pride

Assessment of functional overlap between mouse Dux and human DUX4 in vitro and in vivo

Project description:We report both DUX4 and Dux toxicity depend upon their ability to bind DNA and activate transcription. Chromatin immunoprecipitation of V5 epitope tagged human DUX4 and mouse Dux was performed in human myoblasts was analyzed using ChIP-Seq to identify their subsequent binding sites. We found that DUX4 and Dux bind 4-8% of identical sequences, while majority of the binding sites are unique to either DUX4 or Dux. Although small, this overlap could be due to their conserved abilioty to regualte primordial pathways that were essential for life and therefore maintained in both proteins despite their separate evolutionary paths. We performed ChIP-Seq analysis of human myoblasts transfected with plasmids encoding either epitope tagged human DUX4 (1 sample) and mouse Dux (1 sample). Illumina sequencing libraries were prepared from the ChIP and Input DNA, then resulting DNA libraries were quantified and sequenced and aligned to the human genome (hg19).

2015-12-11 | E-GEOD-75791 | biostudies-arrayexpress

Mouse Dux is myotoxic and shares partial functional homology with its human paralog DUX4

Project description:We report the RNA-seq experiments performed in human myoblasts transfected with human DUX4 and mouse Dux. Comparison of genes up- and down-regulated by DUX4 and Dux in human myoblasts to identify pathways similiarly regulated by both transcription factors.

2016-08-24 | E-GEOD-85935 | biostudies-arrayexpress

Canine Polarized Macrophages Express Distinct Functional and Transcriptomic Profiles

Project description:in the present study we investigate polarized canine macrophages using transcriptome sequencing, a larger panel of flow cytometry markers, and antimicrobial functional assays. Transcriptome analysis of primary canine monocyte-derived macrophages revealed unique, previously unreported signatures for polarized M1 and M2 macrophages.

2022-09-30 | GSE207661 | GEO

DUX4 recruits p300/CBP through its C-terminus and induces global H3K27 acetylation changes

Project description:Ectopic expression of the double homeodomain transcription factor DUX4 causes facioscapulohumeral muscular dystrophy (FSHD). Mechanisms of action of DUX4 are currently unknown. Using immortalized human myoblasts with a titratable DUX4 transgene, we identify by mass spectrometry an interaction between the DUX4 C-terminus and the histone acetyltransferases p300/CBP. Chromatin immunoprecipitation shows that DUX4 recruits p300 to its target gene, ZSCAN4, displaces histone H3 from the center of its binding site, and induces H3K27Ac in its vicinity, but C-terminal deleted DUX4 does not. We show that a DUX4 minigene, bearing only the homeodomains and C-terminus, is transcriptionally functional and cytotoxic, and that overexpression of a nuclear targeted C-terminus impairs the ability of WT DUX4 to interact with p300 and to regulate target genes. Genomic profiling of DUX4, histone H3, and H3 modifications reveals that DUX4 binds two classes of locus: DNase accessible H3K27Ac-rich chromatin and inaccessible H3K27Ac-depleted MaLR-enriched chromatin. At this latter class, it acts as a pioneer factor, recruiting H3K27 acetyltransferase activity and opening the locus for transcription. In concert with local increased H3K27Ac, the strong H3K27Ac peaks at distant sites are significantly depleted of H3K27Ac, thus DUX4 uses its C-terminus to induce a global reorganization of H3K27 acetylation. Two biological samples were analyzed with 4 antibodies for ChIP-Seq and in triplicate for RNA-Seq.

2016-03-10 | E-GEOD-78158 | biostudies-arrayexpress

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