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RNA transcription profile of different yeast mutants under glucose starvation (0.05% glucose)

ABSTRACT: Histone tail modificationscan greatly influencechromatin-associated processes. Asymmetrically modified nucleosomes exist inmultiple cell types; however,whether modifications on both sister histones contribute equally to chromatin dynamicsremainselusive. Here, we devised a bivalent nucleosome system thatallowedfor the constitutive assembly of asymmetrically modified sister histone H3s in nucleosomes inSaccharomyces cerevisiae. The sister H3K36 methylationsaffectedcryptic transcription in gene coding regions, whereassister H3K79 methylation had cooperative effectsongene silencing near telomeres.H3K4 methylation on sister histonesplayed an independent role in suppressing the recruitmentof the Gal4 activator and inhibitingGAL1transcription. Under starvation stress, the expression of glycometabolism pathway geneswasfinetuned by sisterH3K4 methylation.Thus,different modifications on sister histones act either cooperatively or independentlyto regulate transcription in response to external stimuli.

ORGANISM(S): Saccharomyces cerevisiae

PROVIDER: GSE88878 | GEO | 2017/10/16

SECONDARY ACCESSION(S): PRJNA349005

REPOSITORIES: GEO

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RNA transcription profile of different yeast mutants under glucose starvation (0.05% glucose) and comparison of transcriptome of WT and H3D_H3H

Project description:Modifications on histone tails largely affect chromatin associated processes. Previous studies have shown the existence of asymmetrically modified nucleosomes in promoters in multiple cell types. However, whether modifications on both sister histones contribute equally to chromatin dynamics remains elusive. Here we devised a bivalent nucleosome system which allows for the constitutive assembly of asymmetrically modified sister histone H3 in nucleosomes in vivo. We found that the H3K36 methylation on either of sister histones sensitize chromatin structure in gene coding region, while the H3K79 methylation on both sister histone H3s are indispensable for maintaining silent chromatin near telomeres. Additionally, the H3K4 methylation on sister histones plays an equivalent role in suppressing the recruitment of Gal4 activator at GAL1 promoter and GAL1 transcription. Moreover, under starvation stress the expression of a significant proportion of genes in the whole genome is affected by the lack of the H3K4 methylation on one tail of the sister histones, indicating that both sister histones function in fine-tuning transcription through their modifications. We conclude that modifications on sister histones either cooperatively or independently respond to the change of an environmental cue to regulate chromatin structure and function. This work provides a unique experimental strategy to investigate the cross talk between sister histones, and for the first time elaborate their contributions to chromatin in vivo.

2017-10-16 | GSE104312 | GEO

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MARCS: Modification Atlas for Regulation by Chromatin States

Project description:Goal of this project was the identification of chromatin interacting proteins whose binding is differentially regulated by various combinatorial chromatin modifications found in different chromatin states such as promoters, enhancers and heterochromatin. To achieve this, recombinant modified nucleosomes representing different chromatin states were assembled from canonical histones, H2A.Z and modified ligated H3/H4 histone proteins and biotinylated nucleosomal DNAs. Assembled nucleosomes were immobilized on streptavidin-coated beads via biotinylated di-nucleosomal 601 DNA and used for nucleosome affinity purifications to identify proteins regulated by chromatin modifications from SILAC-labelled HeLaS3 nuclear extracts (Arg10 and Lys8). SILAC affinity purifications were carried out in "forward" (heavy extract on modified nucleosome and light extract on unmodified nucleosome) and "reverse" (light extract on modified nucleosome and heavy extract on unmodified nucleosome) label-swap experiments and protein abundances were quantified by MaxQuant. Initial trial experiments with biotinylated mono-, di- and tetra- 601 nucleosomes are also deposited along with the data for the di-nucleosome experiments. See also: Bartke et al., 2010. Nucleosome-interacting proteins regulated by DNA and histone methylation. Cell 143, 470–484; doi:10.1016/j.cell.2010.10.012. The H4K20me2 samples from this experiment were previously deposited with identifier PXD009281. These were published in: Nakamura et al., 2019. H4K20me0 recognition by BRCA1-BARD1 directs homologous recombination to sister chromatids. Nature Cell Biology 21, 311–318; doi: 10.1038/s41556-019-0282-9.

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Independent manipulation of histone H3 modifications in individual nucleosomes reveals the contributions of sister histones to transcription

Project description:Independent manipulation of histone H3 modifications in individual nucleosomes reveals the contributions of sister histones to transcription

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Accurate recycling of parental histones reproduces the histone modification landscape during DNA replication III

Project description:Chromatin organisation is disrupted genome wide during DNA replication. On newly synthesized DNA, nucleosomes are assembled from new naïve histones and old modified histones. It remains unknown whether the landscape of histone post-translational modifications (PTMs) is copied during DNA replication or the epigenomeis perturbed. Here we develop Chromatin Occupancy after Replication, ChOR-seq, a technology that combines chromatin immunopreciptation of histone marks and purification of newly replicated DNA by streptavidin pull-down followed by next generation sequencing. We use this technology to address propagation of epigenetic states across cell division and reveal that accurate recycling of modified parental histones ensures that positional information of histone marks is faithfully reproduced on daughter strands and inherited to daughter cells.

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Accurate recycling of parental histones reproduces the histone modification landscape during DNA replication II

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2018-08-23 | GSE110353 | GEO

Accurate recycling of parental histones reproduces the histone modification landscape during DNA replication

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Effect of glucose refeeding after short-term glucose withdrawal on gene expression of MCF7 cells

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2023-06-29 | GSE206394 | GEO

Density and methylation state of CpG dinucleotides define histone variant specific retention of nucleosomes in mouse spermatozoa

Project description:Nucleosomes are the principal packaging units of chromatin and critical for gene regulation and genome stability. In mammals, a subset of nucleosomes fail to be replaced by protamines during spermatogenesis and are retained in mature spermatozoa providing opportunities for paternal epigenetic transmission. In humans, the remaining 10% localize at regulatory elements of genes. To assess evolutionary conservation and to dissect the molecular logic underlying nucleosome retention, we determined the genome wide nucleosome occupancy in mouse spermatozoa that only contain 1% residual histones. In striking contrast to mammalian somatic cells and haploid round spermatids, we observe high enrichment of nucleosomes at CpG-rich sequences throughout the genome, at conserved regulatory sequences as well as at intra- and intergenic regions and repetitive DNA. This preferred occupancy occurs mutually exclusive with DNA methylation both in mouse and human sperm. At unmethylated CpG-rich sequences, residing nucleosomes are largely composed of the H3.3 histone variant, and trimethylated at lysine 4 (H3K4me3). Both canonical H3.1/H3.2 and H3.3 variant histones are present at promoters marked by Polycomb-mediated H3K27me3, which is strongly predictive for gene repression in pre-implantation embryos. Our data indicate important roles of DNA sequence composition, DNA methylation, variant H3.3 and canonical H3.1/H3.2 histones and associated modifications in nucleosome retention versus eviction during the histone-to-protamine remodeling process in elongating spermatids and potentially in epigenetic inheritance by nucleosomes between generations. Identification of histone, histone variant and histone modification states in round spermatids and sperm

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