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H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles [ATAC-Seq - muscle]

ABSTRACT: H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles [ATAC-Seq - muscle]

PROVIDER: PRJNA625987 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11563821_1.fastq.gz	Fastqsanger.gz
	SRR11563821_2.fastq.gz	Fastqsanger.gz
	SRR11563822_1.fastq.gz	Fastqsanger.gz
	SRR11563822_2.fastq.gz	Fastqsanger.gz
	SRR11563823_1.fastq.gz	Fastqsanger.gz

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H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles

Project description:While the histone variant H2A.Z is known to be required for mitosis, it is also enriched in nucleosomes surrounding the transcription start site of active promoters, implicating H2A.Z in transcription. However, evidence obtained so far mainly rely on correlational data generated in actively dividing cells. We have exploited a paradigm in which transcription is uncoupled from the cell cycle by developing an in vivo system to inactivate H2A.Z in terminally differentiated post-mitotic muscle cells. ChIP-seq, RNA-seq and ATAC-seq experiments performed on H2A.Z KO post-mitotic muscle cells show that this histone variant is neither required to maintain nor to activate transcription. Altogether, this study provides in vivo evidence that in the absence of mitosis H2A.Z is dispensable for transcription and that the enrichment of H2A.Z on active promoters is a marker but not an active driver of transcription.

2019-03-08 | GSE111576 | GEO

H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles [ATAC-Seq - muscle]

2020-04-18 | GSE148865 | GEO

H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles

Project description:H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles

| PRJNA437449 | ENA

H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles [ChIP-Seq - muscle]

Project description:The histone variant H2A.Z is enriched in nucleosomes surrounding the transcription start site of active promoters, suggesting that it might be implicated in transcription. It is also required during mitosis. However, evidences obtained so far mainly rely on correlative evidences obtained in actively dividing cells. We have defined a paradigm in which cell cycle cannot interfere with H2A.Z transcriptional studies by developing an in vivo systems to invalidate H2A.Z in terminally differentiated post-mitotic muscle cells to dissociate its role during transcription from its role during mitosis. ChIP-seq, RNA-seq and ATAC-seq experiments performed on H2A.Z KO post-mitotic muscle cells show that this histone variant is neither required to maintain nor to activate transcription. Altogether, this study provides in vivo evidence that in the absence of mitosis H2A.Z is dispensable for transcription and that the enrichment of H2A.Z on active promoters is rather a marker than an actor of transcriptional activity.

2019-03-08 | GSE111575 | GEO

H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles [RNA-Seq - muscle]

2019-03-08 | GSE111573 | GEO

H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles [ChIP-Seq - muscle]

Project description:H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles [ChIP-Seq - muscle]

| PRJNA437456 | ENA

H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles [RNA-Seq - muscle]

Project description:H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles [RNA-Seq - muscle]

| PRJNA437455 | ENA

H2A.Z is dispensable for both basal and activated transcription in post-mitotic mouse muscles.

| S-EPMC7229818 | biostudies-literature

A cancer-associated mutation in H2A.Z decreases nucleosome stability and impairs mitotic progression

Project description:The histone variant H2A.Z is one of the most evolutionally conserved histone variants. Here, we identified a cancer-associated mutation in H2A.Z and evaluate the mutation. Structural and biochemical in vitro analyses showed that the H2A.Z mutation destabilizes nucleosome containing it. Then we applied the genetic complementation analysis to analyze cellular functions of the H2A.Z mutant. Although the H2A.Z mutant is deposited into nucleosome and rescues the lethality of H2A.Z DKO cells, the mutant does not complement mitotic defects of H2A.Z DKO cells, suggesting that stability of H2A.Z nucleosome is required for proper mitotic progression. Importantly, the H2A.Z mutant led to mitotic defects even in the presence of a larger pool of wild-type H2A.Z. Thus, it is implicated that the cancer-associated mutation appeared in an allele of the H2A.Z isoform genes would be involved in carcinogenesis through causing mitotic defects.

2024-10-28 | GSE84647 | GEO

Genetic complementation analysis revealed distinct contributions of the N-terminal tail of H2A.Z to epigenetic regulations

Project description:The histone variant H2A.Z is one of the most evolutionally conserved histone variants. In vertebrates, two isoforms, H2A.Z.1 and H2A.Z.2, are identified and are involved in multiple epigenetic regulations. However, the role of H2A.Z in epigenetic regulations largely remains unknown especially in vertebrate. Previously, we derived tetracycline-inducible H2A.Z isofmrs double knockout (DKO) cells by using DT40 cells. With this cell, we showed that H2A.Z DKO leads to defects in mitotic progression and gene expression. To elucidate the function of H2A.Z further, we established genetic complementation system and confirmed that introducing exogenous H2A.Z complemented phenotypes of H2A.Z DKO cells. Given that acetylation of the N-terminal tail of H2A.Z reportedly contributes to significant roles in H2A.Z functions, we introduced two types of H2A.Z mutants, non-acetylable H2A.Z (5KR-H2A.Z) and chimeric H2A.Z in which its N-terminal tail is replaced with that of canonical H2A (H2A-H2A.Z), into H2A.Z DKO cells. These H2A.Z mutants complemented defects in mitotic progression. However, significant transcriptional dysregulation was observed in H2A.Z DKO cells stably expressing 5KR-H2A.Z and H2A-H2A.Z. These results suggest that the core domain and the N-terminal tail of the vertebrate H2A.Z contribute individually to mitotic progression and transcription regulation, respectively.

2017-08-21 | GSE70182 | GEO

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