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Localization of histone H3 and histone H3 lysine 4 trimethylation at the start of pre-meiotic S phase

ABSTRACT: ChIP-on-chip analysis of histone H3 and histone H3 lysine 4 trimethylation in cells induced to undergo synchronous meiosis after growth in nitrogen-rich conditions or after nitrogen depletion.

ORGANISM(S): Schizosaccharomyces pombe

PROVIDER: GSE53878 | GEO | 2014/02/20

SECONDARY ACCESSION(S): PRJNA233625

REPOSITORIES: GEO

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Localization of histone H3 and histone H3 lysine 4 trimethylation at the start of pre-meiotic S phase

Project description:ChIP-on-chip analysis of histone H3 and histone H3 lysine 4 trimethylation in cells induced to undergo synchronous meiosis after growth in nitrogen-rich conditions or after nitrogen depletion. Comparison of H3 and H3k4Me3 in diploid pat1-114 cells grown in -N and +N conditions.

2014-02-20 | E-GEOD-53878 | biostudies-arrayexpress

Histone H3 lysine 4 trimethylation marks meiotic recombination initiation sites.

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Histone H3 lysine 27 trimethylation of miRNA genes in HMEC and HMF

Project description:Normal cell type specific histone H3 lysine 27 trimethylation of miRNA genes. HMEC and HMF represent two distinct differentiated cell type present in mammary gland each with a distinct phenotype, a distinct epigenotype as well as distinct miRNA expression pattern. The aim of the study was to determine how epigenetic modifications including histone H3 lysine 27 trimethylation affect miRNA expression. Two cell types HMEC vs. HMF. Biological replicates: 3 pairs of HMEC-HMF of 3 distinct genotypes. Immunoprecipitation using anti-histone H3 trimethylated at lysine 27 (07-449, Millipore).

2011-04-05 | E-GEOD-28376 | biostudies-arrayexpress

Histone H3 lysine 4 trimethylation of miRNA genes in HMEC and HMF

Project description:Normal cell type specific histone H3 lysine 4 trimethylation of miRNA genes. HMEC and HMF represent two distinct differentiated cell type present in mammary gland each with a distinct phenotype, a distinct epigenotype as well as distinct miRNA expression pattern. The aim of the study was to determine how epigenetic modifications including histone H3 lysine 4 trimethylation affect miRNA expression. Two cell types HMEC vs. HMF. Biological replicates: 3 pairs of HMEC-HMF of 3 distinct genotypes. Immunoprecipitation using anti-histone H3 trimethylated at lysine 4 (05-745, Upstate).

2011-04-05 | E-GEOD-28377 | biostudies-arrayexpress

Meiotic time course of Histone H3 occupancy

Project description:To study the meiotic dynamic of the methylation of H3K4, in relation with the transcriptomic regulation, we determine the meiotic time-course of H3 occupancy by ChIP-chip. Keywords: ChIP-chip, meiotic time course, histone modification Strain ORD7339 meiotic time-course from 0 to 6h. Immunoprecipitation with rabbit polyclonal anti H3Cter (Abcam #1791)

2010-05-17 | E-GEOD-10836 | biostudies-arrayexpress

Quantitative histone mass spectrometry identifies elevated histone H3 lysine 27 trimethylation in melanoma

Project description:Normal cell growth is characterized by a regulated epigenetic program that drives cellular activities such as gene transcription, DNA replication and DNA damage repair. Perturbation of this epigenetic program can lead to events such as mis-regulation of gene transcription and diseases such as cancer. To begin to understand the epigenetic program correlated to the development of melanoma, we performed a quantitative mass spectrometric analysis of histone posttranslational modifications mis-regulated in melanoma cell culture. Aggressive melanoma cells were found to have elevated histone H3 lysine 27 trimethylation (H3K27me3) as well as over-expressed methyltransferase EZH2 that adds the specific modification. The altered epigenetic program that led to elevated H3K27me3 in melanoma cell culture was found to directly silence transcription of the tumor suppressor gene RUNX3. The elevated level of H3K27me3 and silencing of RUNX3 transcription was also validated in advanced stage human melanoma tissues. The study presented underscores the utility of using high resolution mass spectrometry to identify mis-regulated epigenetic programs in diseases such as cancer, which could ultimately lead to the identification of biological markers for diagnostic and prognostic applications.

2015-12-02 | PXD002471 | Pride

Meiotic time course of Histone H3 occupancy

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Histone H3 K36 trimethylation in wild-type BY4741 yeast strains

Project description:ChIP-on chip assays to measure the change in histone H3 K36 trimethylation over the yeast genome in wild-type yeast strains.

2012-07-25 | GSE37105 | GEO

Histone H3 K36 trimethylation in wild-type BY4741 yeast strains

Project description:ChIP-on chip assays to measure the change in histone H3 K36 trimethylation over the yeast genome in wild-type yeast strains. Two color experiment.WT cells. Biological replicates=3 per IP per cell type.

2012-07-24 | E-GEOD-37105 | biostudies-arrayexpress

Histone H3 lysine9 acetylation, rather than lysine4 trimethylation, marks meiotic recombination hotspots and promotes recombination initiation in fission yeast

Project description:Histone modifications are associated with meiotic recombination hotspots, discrete sites with augmented recombination frequency. For example, trimethylation of histone H3 lysine4 (H3K4me3) marks most hotspots in budding yeast and mouse. Modified histones are known to regulate meiotic recombination partly by promoting DNA double strand break (DSB) formation, but the role and precise landscape of histone modifications at hotspots remain unclear. Here, we studied hotspot-associated modifications in fission yeast and found general features: acetylation of H3 lysine9 (H3K9ac) is strikingly elevated, and H3K4me3 is not significantly enriched. Remarkably, elimination of H3K9ac reduced binding of the DSB-inducing enzyme Rec12 and DSB at hotspots. We also found that the H3K4 metyltransferase Set1 promotes DSB formation at some loci, but it restricts Rec12 binding to hotspots. These results suggest that H3K9ac rather than H3K4me3 is a hotspot-associated mark involved in meiotic DSB formation in fission yeast.

2013-03-07 | GSE31648 | GEO

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