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Genome-wide analysis of histone trimethylation in INMA cohort exposed to BPA revealed a global impact on telomeric binding proteins and histone acetyltransferase factors

ABSTRACT: Genome-wide analysis of histone trimethylation in INMA cohort exposed to BPA revealed a global impact on telomeric binding proteins and histone acetyltransferase factors

PROVIDER: PRJNA876934 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR21424551.fastq.gz	Fastqsanger.gz
	SRR21424552.fastq.gz	Fastqsanger.gz
	SRR21424553.fastq.gz	Fastqsanger.gz
	SRR21424554.fastq.gz	Fastqsanger.gz
	SRR21424555.fastq.gz	Fastqsanger.gz

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Genome-wide analysis of histone trimethylation in INMA cohort exposed to BPA revealed a global impact on telomeric binding proteins and histone acetyltransferase factors

Project description:This study was developed under the framework of the Human Biomonitoring for Europe Initiative (HBM4EU). We evaluated the possible impacts of BPA exposure in adolescent males from the INMA-Granada cohort (Spain) with the goal of identifying new biomarkers that could be useful in biomonitoring and epidemiological studies. Our hypothesis is that alterations in epigenetic regulation could lead to genetic instability in human subjects exposed to environmentally relevant doses of BPA.

2022-11-16 | GSE212713 | GEO

Histone H4K20 Trimethylation is Decreased in Murine Models of Heart Disease

Project description:Heart disease is the leading cause of death in the developed world, and its comorbidities such as hypertension, diabetes, and heart failure are accompanied by major transcriptomic changes in the heart. During cardiac dysfunction, which leads to heart failure, there are global epigenetic alterations to chromatin that occur concomitantly with morphological changes in the heart in response to acute and chronic stress. These epigenetic alterations include the reversible methylation of lysine residues on histone proteins. Lysine methylation on histone H3K4 and H3K9 were among the first methylated lysine residues identified and have been linked to gene activation and silencing, respectively. However, much less is known regarding other methylated histone residues, including histone H4K20. Trimethylation of histone H4K20 has been shown to repressive gene expression, however this mark has never been examined in the heart. Here we utilized immunoblotting and mass spectrometry to quantify histone H4K20 trimethylation in three models of cardiac dysfunction. Our results show that lysine methylation at this site is regulated in a biphasic manner leading to increased H420 trimethylation during acute hypertrophic stress and decreased H4K20 trimethylation during sustained ischemic injury and cardiac dysfunction. In addition, we examined publicly available datasets to analyze enzymes that regulate H4K20 methylation and identified one demethylase (KDM7C) and two methyltransferases (KMT5A and SMYD5) which were all upregulated in heart failure patients. This is the first study to examine histone H4K20 trimethylation in the heart and to determine how this post-translational modification is differentially regulated in multiple models of cardiac disease.

2022-10-14 | PXD031617 | Pride

Metabolic adaptations underpin resistance to histone acetyltransferase inhibition

Project description:Metabolic adaptations underpin resistance to histone acetyltransferase inhibition

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SMYD5 catalyzes histone H3 lysine 36 trimethylation at promoters

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

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Mammalian telomeres reforged with non-telomeric sequences

Project description:Telomere is a highly refined system for maintaining the stability of linear chromosomes. Most telomeres rely on simple repetitive sequences and telomerase enzymes, but in some species or telomerase-defective situations, alternative telomere lengthening (ALT) mechanism is utilized to protect chromosomal ends. Telomere loss can induce telomere recombination by which specific sequences can be recruited into telomeres. However, canonical telomeric repeat-based telomeres have been found in mammals. Here, we show that mammalian telomeres can also be completely reconstituted using a non-telomeric unique sequence. We found that a specific subtelomeric element, named as mouse template for ALT (mTALT), is utilized for repairing telomeric DNA damage and composing new telomeric sequences in mouse embryonic stem cells. We found a high-level of non-coding mTALT transcript despite the heterochromatic nature of mTALT-based telomere. After ALT activation, the increased HMGN1, a non-histone chromosomal protein, contributed to maintaining telomere stability by regulating telomeric transcriptions. Our findings reveal novel molecular features of potential telomeric sequences which can reconstitute telomeres during cancer formation and evolution.

2020-07-17 | MSV000085772 | MassIVE

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).

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Metabolic adaptations underpin resistance to histone acetyltransferase inhibition [QUANTseq]

Project description:Metabolic adaptations underpin resistance to histone acetyltransferase inhibition [QUANTseq]

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Metabolic adaptations underpin resistance to histone acetyltransferase inhibition [SLAMseq]

Project description:Metabolic adaptations underpin resistance to histone acetyltransferase inhibition [SLAMseq]

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Metabolic adaptations underpin resistance to histone acetyltransferase inhibition [CRISPR]

Project description:Metabolic adaptations underpin resistance to histone acetyltransferase inhibition [CRISPR]

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