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The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE227941 | GEO | 2024/03/01

REPOSITORIES: GEO

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The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking [Hi-C]

Project description:Nucleoskeleton is generally considered to be the grid structure involved in regulation of genome expression and maintenance in the eukaryotic nucleus. However, its actual biological functions and mechanisms remain controversial. Here, we show the nuclear mitotic apparatus protein (NuMA), an essential regulator of the spindle, serve as one of the components of nucleoskeleton to regulates genome high-order architecture. In the interphase, fast depletion of NuMA leads to changes in chromatin organization, including increased accessibility of the genome, remodeling of nucleosome fibers and changes of transcription levels in certain heterochromatin regions. These effects are probably due to NuMA and linker histone H1’s interplay. We prove that NuMA interacts with linker histone H1 and linker DNA through its C-terminal domain. Such interaction facilitates H1’s binding to DNA and promotes nucleosome stacking, and might be part of the reason that NuMA maintains the local condensed state of heterochromatin. Collectively, our results reveal new biological functions of NuMA in the interphase, and also associates nucleoskeleton with genome organization at the mono-nucleosome level for the first time. This in-depth study on the mechanism of NuMA’s regulation on H1 and nucleosomes shed new light on how nucleoskeleton regulates genome architecture and gene expression.

2024-03-01 | GSE227705 | GEO

The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking [ATAC-Seq]

2024-03-01 | GSE227940 | GEO

The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking [RNA-Seq]

2024-03-01 | GSE227707 | GEO

The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking [Cut & Tag]

2024-03-01 | GSE227704 | GEO

The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking

Project description:The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking

| PRJNA947538 | ENA

The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking [RNA-Seq]

Project description:The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking [RNA-Seq]

| PRJNA946693 | ENA

The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking [Hi-C]

Project description:The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking [Hi-C]

| PRJNA946684 | ENA

The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking [Cut & Tag]

Project description:The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking [Cut & Tag]

| PRJNA946679 | ENA

The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking [ATAC-Seq]

Project description:The nucleoskeleton protein NuMA maintains local chromatin architecture partially through promoting linker histone H1’ binding to chromatin and nucleosome stacking [ATAC-Seq]

| PRJNA947543 | ENA

A nucleosome-free region locally abrogates histone H1-dependent restriction of linker DNA accessibility in chromatin.

Project description:Eukaryotic genomes are packaged into linker-oligonucleosome assemblies, providing compaction of genomic DNA and contributing to gene regulation and genome integrity. To define minimal requirements for initial steps in the transition of compact, closed chromatin to a transcriptionally active, open state, we developed a model in vitro system containing a single, unique, "target" nucleosome in the center of a 25-nucleosome array and evaluated the accessibility of the linker DNA adjacent to this target nucleosome. We found that condensation of H1-lacking chromatin results in ?60-fold reduction in linker DNA accessibility and that mimics of acetylation within all four core histone tail domains of the target nucleosome synergize to increase accessibility ?3-fold. Notably, stoichiometric binding of histone H1 caused >2 orders of magnitude reduction in accessibility that was marginally diminished by histone acetylation mimics. Remarkably, a nucleosome-free region (NFR) in place of the target nucleosome completely abrogated H1-dependent restriction of linker accessibility in the immediate vicinity of the NFR. Our results suggest that linker DNA is as inaccessible as DNA within the nucleosome core in fully condensed, H1-containing chromatin. They further imply that an unrecognized function of NFRs in gene promoter regions is to locally abrogate the severe restriction of linker DNA accessibility imposed by H1s.

| S-EPMC6302178 | biostudies-literature

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