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The linker histone H1.0 generates epigenetic and functional intratumor heterogeneity [ChIP-Seq]

ABSTRACT: Identification of enrichment for H3K27ac and H3K27me3 in in vitro generated CSCs, following the knockdown of the histone linker H1.0

ORGANISM(S): Homo sapiens

PROVIDER: GSE73580 | GEO | 2016/09/30

SECONDARY ACCESSION(S): PRJNA297354

REPOSITORIES: GEO

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The linker histone H1.0 generates epigenetic and functional intratumor heterogeneity [FAIRE-Seq]

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The linker histone H1.0 generates epigenetic and functional intratumor heterogeneity

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Genome Wide Distribution of Linker Histone H1.0 is Independent of MeCP2 II

Project description:Previous studies suggested that MeCP2 binds to linker DNA and competes with linker histone H1 to regulate chromatin structure, but this hypothesis has never been tested in vivo. Here, we expressed Flag-tagged H1.0 in forebrain excitatory neurons in mice and performed ChIP-Seq to reveal H1.0 distribution and its relationship with MeCP2. Unexpectedly, we detected no major change in H1.0 upon MeCP2 depletion, revealing that MeCP2 functions independent of linker H1.0.

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Genome Wide Distribution of Linker Histone H1.0 is Independent of MeCP2 I

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Linker Histone H1.0 Couples Cellular Stiffness to Chromatin Structure [RNA-seq]

Project description:Eukaryotic nuclei encase the genome and differentially package it for the various needs of distinct cell types. Tuning of genome structure and function is accomplished by chromatin binding proteins, which are responsive to cellular stress, determining the transcriptome and phenotype of the cell. We sought to investigate the connection between extracellular stress and chromatin structure to regulate cellular stiffness. We demonstrate that the linker histone H1.0, which compacts nucleosomes into higher order chromatin fibers, controls genome structure and cellular response to stress. Histone H1.0 has privileged expression in tension-responsive fibroblasts across tissue types in mouse and humans, and is necessary and sufficient to mount a myofibroblast phenotype in these cells. Loss of histone H1.0 prevents transforming growth factor beta (TGF-b)-induced fibroblast contraction, proliferation and migration in an isoform-specific manner via inhibition of a transcriptome targeting extracellular matrix molecules. Histone H1.0 is associated with local regulation of gene expression by chromatin fiber compaction and histone acetylation, rendering the nucleus and cell stiffer in response to cytokine stimulation. Knockdown of H1.0 decreased levels of HDAC1 and the chromatin reader BRD4, thereby preventing transcription of a fibrotic gene program. Transient depletion of histone H1.0 in vivo decompacts chromatin and prevents fibrosis in cardiac muscle, lung, and kidney, thereby linking chromatin structure with fibroblast phenotype in response to extracellular stress. Our work identifies an unexpected role of linker histones to sense and respond to cellular stress, directly coupling cellular tension, nuclear organization and gene transcription.

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Linker Histone H1.0 Couples Cellular Stiffness to Chromatin Structure [ChIP-seq]

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Dynamic regulation of the histone variant H1.0 contributes to intratumor epigenetic and functional heterogeneity [RNA-Seq]

Project description:Identification of genes regulated by the histone variant H1.0 by RNA-seq analysis of cell lines expressing inducible specific shRNAs.

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Identification and analysis of phosphorylation within Xenopus laevis linker histone H1.0

Project description:As a key structural component of the chromatin of higher eukaryotes, linker histones (H1s) are involved in stabilizing the folding of extended nucleosome arrays into higher-order chromatin structures and function as a gene-specific regulators of transcription in vivo. The H1 C-terminal domain (CTD) is essential for high affinity binding of linker histones to chromatin and stabilization of higher-order chromatin structure. Importantly, the H1 CTD is an intrinsically disordered domain that undergoes a drastic condensation upon binding to nucleosomes. Moroever, although phosphorylation is a prevalent posttranslational modification (PTM) within the H1 CTD, exactly where this modification is installed and how phosphorylation influences the structure of the H1 CTD remains unclear for many H1s. Using novel mass spectrometry techniques, we identified six phosphorylation sites within the CTD of the archetypal linker histone Xenopus H1.0. We then analyzed nucleosome-dependent CTD condensation and H1-dependent linker DNA conformation for six full-length H1s in which the phosphorylated serine residues were replaced by glutamic acid residues.

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