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Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes

ABSTRACT: Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes

PROVIDER: PRJNA657058 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12450414.fastq.gz	Fastqsanger.gz
	SRR12450415.fastq.gz	Fastqsanger.gz
	SRR12450318_1.fastq.gz	Fastqsanger.gz
	SRR12450318_2.fastq.gz	Fastqsanger.gz
	SRR12450319_1.fastq.gz	Fastqsanger.gz

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Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes (ATAC-seq_DRB)

Project description:Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes (ATAC-seq_DRB)

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Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes (ATAC-seq)

Project description:Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes (ATAC-seq)

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Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes (ChIP-seq)

Project description:Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes (ChIP-seq)

| PRJNA657059 | ENA

Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes (ChIP-seq)

Project description:To study the role of Histone H4 lysine 20 mono- and tri-methylation (H4K20me1, H4K20me3) in relationship to chromatin accessibility and gene expression, we report the application of high-throughput profiling of these marks in Human Osteosarcoma U2OS and Mouse Fibroblast (MEF) cells with Set8 knockdown or control siRNA treatment. We find that H4K20me1 contributes to the open chromatin structure at active genes.

2021-06-04 | GSE156216 | GEO

Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes (ATAC-seq)

Project description:To study the role of Histone H4 lysine 20 mono- and tri-methylation (H4K20me1, H4K20me3) in relationship to chromatin accessibility and gene expression, we report the application of high-throughput profiling of these marks in synchronized and asynchronous Human Osteosarcoma U2OS and asynchronous Mouse Fibroblast (MEF) cells with Set8 knockdown or control siRNA treatment. We find that H4K20me1 contributes to the open chromatin structure at active genes.

2021-06-04 | GSE156215 | GEO

Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes (ATAC-seq_DRB)

Project description:To study the role of Histone H4 lysine 20 mono- and tri-methylation (H4K20me1, H4K20me3) in relationship to chromatin accessibility and gene expression, we report the application of high-throughput profiling of these marks in synchronized and asynchronous Human Osteosarcoma U2OS and asynchronous Mouse Fibroblast (MEF) cells with Set8 knockdown or control siRNA treatment. We find that H4K20me1 contributes to the open chromatin structure at active genes.

2021-06-04 | GSE173313 | GEO

Histone H4 lysine 20 mono-methylation directly facilitates chromatin openness and promotes transcription of housekeeping genes.

Project description:Histone lysine methylations have primarily been linked to selective recruitment of reader or effector proteins that subsequently modify chromatin regions and mediate genome functions. Here, we describe a divergent role for histone H4 lysine 20 mono-methylation (H4K20me1) and demonstrate that it directly facilitates chromatin openness and accessibility by disrupting chromatin folding. Thus, accumulation of H4K20me1 demarcates highly accessible chromatin at genes, and this is maintained throughout the cell cycle. In vitro, H4K20me1-containing nucleosomal arrays with nucleosome repeat lengths (NRL) of 187 and 197 are less compact than unmethylated (H4K20me0) or trimethylated (H4K20me3) arrays. Concordantly, and in contrast to trimethylated and unmethylated tails, solid-state NMR data shows that H4K20 mono-methylation changes the H4 conformational state and leads to more dynamic histone H4-tails. Notably, the increased chromatin accessibility mediated by H4K20me1 facilitates gene expression, particularly of housekeeping genes. Altogether, we show how the methylation state of a single histone H4 residue operates as a focal point in chromatin structure control. While H4K20me1 directly promotes chromatin openness at highly transcribed genes, it also serves as a stepping-stone for H4K20me3-dependent chromatin compaction.

| S-EPMC8379281 | biostudies-literature

Histone H4 lysine 20 mono-methylation directly facilitates chromatin ‘openness’ and promotes transcription of housekeeping genes

Project description:This SuperSeries is composed of the SubSeries listed below.

2021-06-04 | GSE156217 | GEO

MALDI-TOF Profiling of modified histone proteins

Project description:Histone lysine methylations as one of the chromatin post-translational modifications, has been linked to the modification of chromatin regions and mediating genome functions.In this study, we investigated the divergent role for histone H4 lysine 20 mono-methylation (H4K20me1) in facilitates chromatin openness and accessibility by disrupting chromatin folding.

2021-08-26 | PXD027150 | Pride

Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics

Project description:Chromatin is decorated with diverse histone posttranslational modifications (PTMs) that are involved in regulating chromatin structure and dynamics during various DNA-associated processes such as gene transcription, DNA replication and DNA damage repair. Here, we combine a chemical reporter with mass spectrometry to identify a new class of histone PTM, lysine glutarylation (Kglu), occurring at 27 lysine residues on human core histones. The characterization of an evolutionarily conserved Kglu mark at histone H4 lysine 91 (H4K91glu) using a semisynthetic glutarylated protein reveals that this negatively charged modification greatly destabilizes nucleosome by weakening the interactions between histone H2A/H2B dimers and H3/H4 tetramer in vitro. The replacement of H4K91 by glutamic acid in S. cerevisiae to mimic glutarylation influences chromatin structure and thereby results in a global up-regulation of transcription and defects in cell cycle progression, DNA damage repair and telomere silencing in vivo. In mammalian cells, H4K91glu is mainly enriched at promoter regions of highly expressed genes. A down-regulation of H4K91glu is tightly associated with chromatin condensation during mitosis and in response to DNA damage. The cellular dynamics of H4K91glu is controlled by Sirt7 as a deglutarylase and KAT2A as a glutaryltransferase. This study designates a new histone mark (Kglu) as a new regulatory mechanism for chromatin dynamics.

2019-09-16 | GSE131807 | GEO

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