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DUX4-induced histone variants H3.X and H3.Y mark DUX4 target genes for expression (CUT&RUN)

ABSTRACT: DUX4-induced histone variants H3.X and H3.Y mark DUX4 target genes for expression (CUT&RUN)

PROVIDER: PRJNA489182 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR7781300_1.fastq.gz	Fastqsanger.gz
	SRR7781300_2.fastq.gz	Fastqsanger.gz
	SRR7781301_1.fastq.gz	Fastqsanger.gz
	SRR7781301_2.fastq.gz	Fastqsanger.gz
	SRR7781302_1.fastq.gz	Fastqsanger.gz

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DUX4-induced histone variants H3.X and H3.Y mark DUX4 target genes for expression (CUT&RUN)

Project description:We determined the effects of short pulses of DUX4 expression on genome-wide transcription, mimicking the embryonic expression of this gene, using a DUX4-inducible cell culture model of FSHD (MB135iDUX4). We found that a second pulse of DUX4 has a synergistic effect and shows greater induction of DUX4 targets. Knockdown of DUX4-induced histone variants H3.X and H3.Y has no effect on DUX4 targets with a single pulse of DUX4 but eliminates the superinduction seen with a second pulse, showing that these histones are required for this increase in expression.

2019-08-31 | GSE119401 | GEO

DUX4-induced histone variants H3.X and H3.Y mark DUX4 target genes for expression

Project description:DUX4-induced histone variants H3.X and H3.Y mark DUX4 target genes for expression

| PRJNA489180 | ENA

DUX4-induced histone variants H3.X and H3.Y mark DUX4 target genes for expression (RNA-seq)

2019-08-31 | GSE119402 | GEO

DUX4-induced histone variants H3.X and H3.Y mark DUX4 target genes for expression (RNA-seq)

Project description:DUX4-induced histone variants H3.X and H3.Y mark DUX4 target genes for expression (RNA-seq)

| PRJNA489184 | ENA

DUX4-Induced Histone Variants H3.X and H3.Y Mark DUX4 Target Genes for Expression.

Project description:The DUX4 transcription factor is briefly expressed in the early cleavage-stage embryo, where it induces an early wave of zygotic gene transcription, whereas its mis-expression in skeletal muscle causes the muscular dystrophy facioscapulohumeral dystrophy (FSHD). Here, we show that DUX4 induces the expression of the histone variants H3.X and H3.Y. We have used a myoblast cell line with doxycycline-inducible DUX4 to show that these histone variants are incorporated throughout the body of DUX4-induced genes. Following a brief pulse of DUX4, these histones contribute to greater perdurance and to enhanced re-activation of DUX4 target gene expression. These findings provide a model for H3.X/Y as a chromatin mechanism that facilitates the expression of DUX4 target genes subsequent to a brief pulse of DUX4 expression.

| S-EPMC6886682 | biostudies-literature

CUT & RUN analysis of H3K4me2 mark upon LSD1 inhibition

Project description:CUT & RUN analysis of H3K4me2 mark upon LSD1 inhibition

| PRJNA985560 | ENA

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

DUX4-induced histone variants H3.X and H3.Y mark DUX4 target genes for expression

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

2019-08-31 | GSE119403 | GEO

Histone H3 proline 16 hydroxylation regulates mammalian gene expression [CUT&RUN]

Project description:Histone H3 proline 16 hydroxylation regulates mammalian gene expression [CUT&RUN]

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CUT & RUN analysis of H3K4me2 mark upon LSD1 inhibition

Project description:Lysine-specific demethylase 1 (LSD1) is a histone demethylase that promotes stemness and cancer cell survival, including in prostate cancer. LSD1 has been shown to perfrom catalytic independent function sto promote prostate cancer survival. Here, we tested the levels of LSD1's canonical target H3K4me2 upon LSD1 inhibition with SP2509 across the genome using CUT and RUN analysis.

2023-08-30 | GSE235211 | GEO

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