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Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2

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

ORGANISM(S): Homo sapiens

PROVIDER: GSE239447 | GEO | 2023/12/11

REPOSITORIES: GEO

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Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2

Project description:Polycomb repressive complex 2 (PRC2) interacts with RNAs in cells, but there is no consensus on how RNA regulates its canonical functions, including chromatin modification and the maintenance of transcription programs in lineage-committed cells. We assayed two separation-of-function mutants of the catalytic subunit EZH2, defective in RNA binding but active in methyltransferase. We find that part of the RNA-binding surface of EZH2 is required for chromatin modification, yet this activity is independent of RNA. Mechanistically, the RNA-binding surface within EZH2 is required for chromatin modification in vitro and in cells, through interactions with nucleosomal DNA. Contrarily, an RNA-binding defective mutant exhibited normal chromatin modification activity in vitro and in lineage-committed cells, accompanied by normal gene repression activity. Collectively, we show that part of the RNA-binding surface of PRC2, rather than the RNA-binding activity per se, is required for the histone methylation of chromatin in vitro and in cells.

2023-12-11 | GSE199543 | GEO

Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2 [ChIP-seq]

2023-12-11 | GSE239445 | GEO

Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2

Project description:Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2

| PRJNA999315 | ENA

Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2

Project description:Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2

| PRJNA820710 | ENA

Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2 [ChIP-seq]

Project description:Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2 [ChIP-seq]

| PRJNA999319 | ENA

Nucleosome-binding activities within JARID2 and EZH1 regulate the function of PRC2 on chromatin.

Project description:Polycomb-repressive complex 2 (PRC2) comprises specific members of the Polycomb group of epigenetic modulators. PRC2 catalyzes methylation of histone H3 at Lys 27 (H3K27me3) through its Enhancer of zeste (Ezh) constituent, of which there are two mammalian homologs: Ezh1 and Ezh2. Several ancillary factors, including Jarid2, modulate PRC2 function, with Jarid2 facilitating its recruitment to target genes. Jarid2, like Ezh2, is present in poorly differentiated and actively dividing cells, while Ezh1 associates with PRC2 in all cells, including resting cells. We found that Jarid2 exhibits nucleosome-binding activity that contributes to PRC2 stimulation. Moreover, such nucleosome-binding activity is exhibited by PRC2 comprising Ezh1 (PRC2-Ezh1), in contrast to PRC2-Ezh2. The presence of Ezh1 helps to maintain PRC2 occupancy on its target genes in myoblasts where Jarid2 is not expressed. Our findings allow us to propose a model in which PRC2-Ezh2 is important for the de novo establishment of H3K27me3 in dividing cells, whereas PRC2-Ezh1 is required for its maintenance in resting cells.

| S-EPMC3877756 | biostudies-literature

PGE2 alters chromatin through H2A.Zvariant enhancer nucleosome modification to promote hematopoietic stem cell fate

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

2024-06-10 | GSE229399 | GEO

The ATP-dependent chromatin remodeling enzymes CHD6, CHD7, and CHD8 exhibit distinct nucleosome binding and remodeling activities.

Project description:Proper chromatin regulation is central to genome function and maintenance. The group III chromodomain-helicase-DNA-binding (CHD) family of ATP-dependent chromatin remodeling enzymes, comprising CHD6, CHD7, CHD8, and CHD9, has well-documented roles in transcription regulation, impacting both organism development and disease etiology. These four enzymes are similar in their constituent domains, but they fill surprisingly non-redundant roles in the cell, with deficiencies in individual enzymes leading to dissimilar disease states such as CHARGE syndrome or autism spectrum disorders. The mechanisms explaining their divergent, non-overlapping functions are unclear. In this study, we performed an in-depth biochemical analysis of purified CHD6, CHD7, and CHD8 and discovered distinct differences in chromatin remodeling specificities and activities among them. We report that CHD6 and CHD7 both bind with high affinity to short linker DNA, whereas CHD8 requires longer DNA for binding. As a result, CHD8 slides nucleosomes into positions with more flanking linker DNA than CHD7. Moreover, we found that, although CHD7 and CHD8 slide nucleosomes, CHD6 disrupts nucleosomes in a distinct non-sliding manner. The different activities of these enzymes likely lead to differences in chromatin structure and, thereby, transcriptional control, at the enhancer and promoter loci where these enzymes bind. Overall, our work provides a mechanistic basis for both the non-redundant roles and the diverse mutant disease states of these enzymes in vivo.

| S-EPMC5512084 | biostudies-literature

Nucleosome driven transcription factor binding and gene regulati

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2012-12-01 | E-GEOD-41617 | biostudies-arrayexpress

A charged and contoured surface on the nucleosome regulates chromatin compaction.

Project description:Local nucleosome-nucleosome interactions in cis drive chromatin folding, whereas interactions in trans lead to fiber-fiber oligomerization. Here we show that peptides derived from the histone H4 tail and Kaposi's sarcoma herpesvirus LANA protein can replace the endogenous H4 tail, resulting in array folding and oligomerization. Neutralization of a LANA binding site on the histone surface enhanced rather than abolished nucleosome-nucleosome interactions. We maintain that the contoured nucleosome surface is centrally involved in regulating chromatin condensation.

| S-EPMC2366819 | biostudies-literature

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