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The linker histone H1.2 directs the genome-wide chromatin-association and facilitates the biological effects of the retinoblastoma tumour suppressor protein

ABSTRACT: ChIPseq of Retinoblastoma protein in MCF7 cells in which linker histone H1.2 has been knocked down.

ORGANISM(S): Homo sapiens

PROVIDER: GSE98728 | GEO | 2017/06/13

SECONDARY ACCESSION(S): PRJNA386040

REPOSITORIES: GEO

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Linker histone H1.2 establishes chromatin comapction and gene silencing through recognition of H3K27me3

Project description:Linker histone H1 is a protein component of chromatin and has been linked to chromatin compaction and global gene silencing.It has been sugegsted that H1 plays a significant role, regulating a relatively small number of genes. Here we show that H1.2- a variant of H1 subtype is recruited to chromatin region and is dependent on EZH2-mediated H3K27me3. Therefore a Gene expression array analysis was carried out with H1.2 as well as EZH2 knockout MCF7 cells to confirm the interlationship of H1.2 and EZH2 activity. Total RNA was isolated from MCF7 cells in which EZH2 and H1.2 genes have been depleted along with the wild type cells to study the differential regulation of various genes in each case.

2015-12-21 | E-GEOD-68050 | biostudies-arrayexpress

Linker histone H1.2 establishes chromatin comapction and gene silencing through recognition of H3K27me3

2015-12-21 | GSE68050 | GEO

ChIP-seq for histone H1.2 in A549

Project description:Our study represents the detailed analysis of whole-genome DNA-binding sites of linker histone variant H1.2 in human lung cancer cell line A549, with biologic replicates, generated by ChIP-seq technology

2023-08-30 | GSE237852 | GEO

Interactome of intact chromatosome variants with site-specifically ubiquitylated and acetylated linker histone H1.2

Project description:Post-translational modifications (PTMs) of histones have fundamental effects on chromatin structure and function. While the impact of PTMs on the function of core histones are increasingly well understood, this is much less the case for modifications of linker histone H1, which is at least in part due to a lack of proper tools. In this work, we establish the assembly of intact chromatosomes containing site-specifically ubiquitylated and acetylated linker histone H1.2 variants obtained by a combination of chemical biology approaches. We then use these complexes in a tailored affinity enrichment mass spectrometry workflow to identify and comprehensively characterize chromatosome-specific cellular interactomes and the impact of site-specific linker histone modifications on a proteome-wide scale. We validate and benchmark our approach by western-blotting and by confirming the involvement of chromatin-bound H1.2 in the recruitment of proteins involved in DNA double-strand break repair using an in vitro ligation assay. We relate our data to previous work and in particular compare it to data on modification-specific interaction partners of free H1. Taken together, our data supports the role of chromatin-bound H1 as a regulatory protein with distinct functions beyond DNA compaction and constitutes an important resource for future investigations of histone epigenetic modifications.

2023-11-02 | PXD040236 | Pride

Linker Histone H1.2 Directs Genome-wide Chromatin Association of the Retinoblastoma Tumor Suppressor Protein and Facilitates Its Function.

Project description: Not available

| S-EPMC5478878 | biostudies-literature

Genome-wide expression profiling in 293T cells upon depletion of H1.2, Cul4A or PAF1

Project description:Increasing evidence suggests that linker histone H1 can influence distinct cellular processes by acting as a gene-specific regulator. However, the mechanistic basis underlying such H1 specificity and whether H1 acts in concert with other chromatin-altering activities remain unclear. To investigate the cooperative role of H1.2, Cul4A and PAF1 on gene regulation, genome-wide gene expression analysis is carried out in 293T cells expressing control shRNA, H1.2 shRNA, Cul4A shRNA or PAF1 shRNA. Total RNA was isolated from 293T cells expressing NCsh, H1.2sh, Cul4Ash, or PAF1sh

2013-12-20 | E-GEOD-52544 | biostudies-arrayexpress

Genome-wide expression profiling in 293T cells upon depletion of H1.2, Cul4A or PAF1

2013-12-20 | GSE52544 | GEO

ChIP-seq for histone H1.2 in iWAT of C57BL/6 mice under normal conditions or upon cold exposure

Project description:Our study represents the detailed analysis of whole-genome DNA-binding sites of linker histone variant H1.2 in iWAT of male C57BL/6 mice under normal conditions or upon cold exposures, with biologic replicates, generated by ChIP-seq technology

2023-06-15 | GSE232530 | GEO

Mapping of somatic linker histone H1 variants in T47D-MTVL cells

Project description:At least six histone H1 variants exist in mammalian somatic cells that bind to the linker DNA and stabilize the nucleosome particle contributing to higher order chromatin compaction. In addition, H1 seems to be involved in the active regulation of gene expression. It is not well known whether the different variants have specific roles, are distributed differentially along the genome, or regulate specific promoters. By taking advantage of specific antibodies to H1 variants and HA-tagged recombinant H1 variants expressed in a breast cancer-derived cell line, we have investigated the distribution of the different somatic H1 variants (H1.2 to H1.5, H1.0 and H1X) in particular promoters and genome-wide. Genome-wide analysis of H1.0, H1.2, H1.4, H1X and H3

2014-02-04 | E-GEOD-49334 | biostudies-arrayexpress

Hormone induced repression of genes requires BRG1-mediated H1.2 deposition at target promoters

Project description:In this report we have discovered a new function of BRG1 during hormone-mediated gene repression. The ATPase BRG1 without the other subunits of the BAF complex is recruited by the hormone receptor to genomic sites marked by the pioneering factor FOXA1, where it remodels the target chromatin by interacting with linker histone H1.2 facilitating its deposition.

2016-07-11 | GSE83785 | GEO

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