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Alcohol induced increases in sperm Histone H3 lysine 4 trimethylation correlate with increased placental CTCF occupancy and altered developmental programming

ABSTRACT: Alcohol induced increases in sperm Histone H3 lysine 4 trimethylation correlate with increased placental CTCF occupancy and altered developmental programming

PROVIDER: PRJNA838979 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR19258963.fastq.gz	Fastqsanger.gz
	SRR19258964.fastq.gz	Fastqsanger.gz
	SRR19258965.fastq.gz	Fastqsanger.gz
	SRR19258966.fastq.gz	Fastqsanger.gz
	SRR19258967.fastq.gz	Fastqsanger.gz

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Alcohol induced increases in sperm Histone H3 lysine 4 trimethylation correlate with increased placental CTCF occupancy and altered developmental programming

Project description:Using a mouse model, studies by our group reveal that paternal preconception alcohol intake affects offspring fetal-placental growth, with long-lasting consequences on adult metabolism. Here, we tested the hypothesis that chronic preconception male alcohol exposure impacts histone enrichment in sperm and that these changes are associated with altered developmental programming in the placenta. Using chromatin immunoprecipitation, we find alcohol-induced increases in sperm histone H3 lysine 4 trimethylation (H3K4me3) that map to promoters and presumptive enhancer regions enriched in genes driving neurogenesis and craniofacial development. Given the colocalization of H3K4me3 with the chromatin binding factor CTCF across both sperm and embryos, we next examined CTCF localization in the placenta. We find global changes in CTCF binding within placentae derived from the male offspring of alcohol-exposed sires. Furthermore, altered CTCF localization correlates with dysregulated gene expression across multiple gene clusters; however, these transcriptional changes only occur in male offspring. Finally, we identified a correlation between genomic regions exhibiting alcohol-induced increases in sperm H3K4me3 and increased CTCF binding in male placentae. Collectively, our analysis demonstrates that the chromatin landscape of sperm is sensitive to chronic alcohol exposure and that a subset of these affected regions exhibits increased placental CTCF enrichment.

2022-05-24 | GSE203189 | GEO

Alcohol induced increases in sperm Histone H3 lysine 4 trimethylation correlate with increased placental CTCF occupancy and altered developmental programming.

| S-EPMC9130987 | biostudies-literature

Epigenetic programming of human sperm

Project description:Epigenetic programming of human sperm

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NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming

Project description:This SuperSeries is composed of the following subset Series: GSE29146: NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming [ChIP] GSE29147: NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming [RNAi] GSE29148: NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming [TKO] GSE29150: NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming [Transduction] Refer to individual Series

2011-11-29 | E-GEOD-29305 | biostudies-arrayexpress

Sperm histone H3 lysine 4 trimethylation is altered in a genetic mouse model of transgenerational epigenetic inheritance

Project description:Advancing the molecular knowledge surrounding fertility and inheritance has become critical given the halving of sperm counts in the last 40 years, and the rise in complex disease which cannot be explained by genetics alone. The connection between both these trends may lie in alterations to the sperm epigenome and occur through environmental exposures. Changes to the sperm epigenome are also associated with health risks across generations such as metabolic disorders and cancer. Thus it is imperative to identify the epigenetic modifications that escape reprogramming during spermatogenesis. Here, we aimed to identify the chromatin signature(s) associated with transgenerational phenotypes in our genetic mouse model of epigenetic inheritance that overexpresses the histone demethylase KDM1A in their germ cells. We used sperm-specific chromatin immunoprecipitation followed by in depth sequencing (ChIP-seq), and computational analysis to identify whether differential enrichment of histone H3 lysine 4 trimethylation (H3K4me3), and histone H3 lysine 27 trimethylation (H3K27me3) serve as mechanisms for transgenerational epigenetic inheritance through the paternal germline. Our analysis on the sperm of KDM1A transgenic males revealed specific changes in H3K4me3 enrichment that occurred independently from non-bivalent H3K4me3/H3K27me3 regions. Many regions with altered H3K4me3 enrichment in sperm were identified on the paternal allele of the pre-implantation embryo. These findings suggest that sperm H3K4me3 functions in the transmission of non-genetic phenotypes transgenerationally.

2020-10-15 | GSE145679 | GEO

Lysine trimethylation in planktonic and pellicle modes of growth in Acinetobacter baumannii

Project description:An increasing number of studies have shown the importance of post-translational modifications (PTM) in bacterial physiology, especially during biofilm formation. Trimethylation of lysine residues is little studied due to lack of specific enrichment methods for this PTM. However, it may have a significant role in virulence, adaptation or biofilm formation. Acinetobacter baumannii has been described as an important nosocomial pathogen over the past 30 years, frequently implicated in ventilator-associated infections. Many aspects of the biology of A. baumannii remain elusive, in particular the formation of an air-liquid biofilm (pellicle). Here, we investigated K-trimethylation in A. baumannii ATCC 17978 in planktonic and pellicle modes by proteomic analysis, using different analytical approaches. Here, we identified 84 K-trimethylated proteins. Among these proteins, several are localized to the membrane or involved in adhesion, biofilm formation, lipid metabolism and even characterized as virulence or resistance factors. Our results confirmed some K-trimethylated sites previously identified in other bacteria, such as three sites on the 50S ribosomal subunit protein L11 (RplK). But we also identified novel sites such as K1020 on the adhesin Ata autotransporter (Ata), which is a known virulence factor and participates in bacterial adhesion. Overall, this study is the first large-scale proteomic study of trimethylation in A. baumannii and will be an important resource for the scientific community.

2023-07-20 | PXD035239 | Pride

Epigenetic homogeneity underlies sperm programming for embryonic transcription

Project description:Epigenetic homogeneity underlies sperm programming for embryonic transcription single-ended ChIP-Seq libraries from sperm, egg extract (-geminin) treated sperm, egg extract (+geminin) treated sperm, and St 7 embryos with antibody for H3Kme3, H3K27me3, 3 replicates for each histone modification pull-down

2020-06-05 | GSE125982 | GEO

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.

2011-04-05 | GSE28377 | GEO

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.

2011-04-05 | GSE28376 | GEO

SMYD5 catalyzes histone H3 lysine 36 trimethylation at promoters

Project description:SMYD5 catalyzes histone H3 lysine 36 trimethylation at promoters

| PRJNA766856 | ENA