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Tip60-mediated H2A.Z acetylation is required for neuronal fate specification and bivalent gene activation [Cut & Tag]

ABSTRACT: Tip60-mediated H2A.Z acetylation is required for neuronal fate specification and bivalent gene activation [Cut & Tag]

PROVIDER: PRJNA753812 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15415100_1.fastq.gz	Fastqsanger.gz
	SRR15415100_2.fastq.gz	Fastqsanger.gz
	SRR15415101_1.fastq.gz	Fastqsanger.gz
	SRR15415101_2.fastq.gz	Fastqsanger.gz
	SRR15415102_1.fastq.gz	Fastqsanger.gz

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Tip60-mediated H2A.Z acetylation promotes neuronal fate specification and bivalent gene activation.

Project description:Tip60-mediated H2A.Z acetylation promotes neuronal fate specification and bivalent gene activation.

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Tip60-mediated H2A.Z acetylation is required for neuronal fate specification and bivalent gene activation [RNA-Seq]

Project description:Tip60-mediated H2A.Z acetylation is required for neuronal fate specification and bivalent gene activation [RNA-Seq]

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Tip60-mediated H2A.Z acetylation is required for neuronal fate specification and bivalent gene activation [ATAC-Seq]

Project description:Tip60-mediated H2A.Z acetylation is required for neuronal fate specification and bivalent gene activation [ATAC-Seq]

| PRJNA754100 | ENA

Tip60-mediated H2A.Z acetylation is required for neuronal fate specification and bivalent gene activation [Cut & Tag]

Project description:Tip60-dependnet histone modification/occupancy dynamics during Ascl1-mediated direct reprogramming of mouse embryonic fibroblasts (MEFs) into induced neuronal cells.

2022-11-22 | GSE181888 | GEO

Tip60-mediated H2A.Z acetylation promotes neuronal fate specification and bivalent gene activation.

Project description:Cell lineage specification is accomplished by a concerted action of chromatin remodeling and tissue-specific transcription factors. However, the mechanisms that induce and maintain appropriate lineage-specific gene expression remain elusive. Here, we used an unbiased proteomics approach to characterize chromatin regulators that mediate the induction of neuronal cell fate. We found that Tip60 acetyltransferase is essential to establish neuronal cell identity partly via acetylation of the histone variant H2A.Z. Despite its tight correlation with gene expression and active chromatin, loss of H2A.Z acetylation had little effect on chromatin accessibility or transcription. Instead, loss of Tip60 and acetyl-H2A.Z interfered with H3K4me3 deposition and activation of a unique subset of silent, lineage-restricted genes characterized by a bivalent chromatin configuration at their promoters. Altogether, our results illuminate the mechanisms underlying bivalent chromatin activation and reveal that H2A.Z acetylation regulates neuronal fate specification by establishing epigenetic competence for bivalent gene activation and cell lineage transition.

| S-EPMC9779922 | biostudies-literature

Tip60-mediated H2A.Z acetylation is required for neuronal fate specification and bivalent gene activation [ATAC-Seq]

Project description:Examination of the effects of Tip60/Kat5 depletion on chromatin accessibility dynamics during Ascl1-mediated direct reprogramming of mouse embryonic fibroblasts (MEFs) into induced neuronal cells.

2022-11-22 | GSE181964 | GEO

Tip60-mediated H2A.Z acetylation is required for neuronal fate specification and bivalent gene activation [RNA-Seq]

Project description:Examination of the effects of Tip60/Kat5 depletion on gene expression dynamics during Ascl1-mediated direct reprogramming of mouse embryonic fibroblasts (MEFs) into induced neuronal cells.

2022-11-22 | GSE181887 | GEO

Gas41 links histone acetylation to H2A.Z deposition and stem cell identity maintenance

Project description:The histone variant H2A.Z is essential for maintaining the identity of embryonic stem cell (ESC) by keeping bivalent developmental genes at a poised state. However, how H2A.Z is deposited into the bivalent domains remains unknown. In mammals, two chromatin-remodeling complexes, Tip60/p400 and SRCAP, exchange the canonical histone H2A for H2A.Z in the chromatin. Here we show that Glioma Amplified Sequence 41 (Gas41), a shared subunit of the two H2A.Z-depositing complexes, functions as a reader of histone acetylation and recruits Tip60/p400 and SRCAP to deposit H2A.Z into specific chromatin regions including bivalent domains. The YEATS domain of Gas41 bound to acetylation on histone H3K27 and H3K14 both in vitro and in cells. Crystal structure of the Gas41 YEATS domain in complex with the H3K27ac peptide revealed that, similar to the AF9 and ENL YEATS domains, Gas41 YEATS forms a serine-lined aromatic cage for Kac recognition; mutations of either the aromatic residues of YEATS domain or the nearby residue of H3K27 abrogated the interaction. In mESCs, knockdown of Gas41 led to cell differentiation as the result of derepression of differentiation genes. Importantly, the differentiated morphology was rescued by expressing wild type Gas41, but not the YEATS domain mutated counterparts that do not recognize histone acetylation. Mechanically, we found that Gas41 depletion led to reduction of H2A.Z levels and a concomitant reduction of H3K27me3 levels at the promoters of a subset of bivalent genes. Together, our study identifies the Gas41 YEATS domain as a reader of histone acetylation and establishes a link between histone acetylation and H2A.Z deposition in the maintenance of ESC identity.

2018-07-01 | GSE100460 | GEO

Tip60-mediated H2A.Z acetylation promotes neuronal fate specification and bivalent gene activation.

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

2022-11-22 | GSE181965 | GEO

Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex

Project description:The human NuA4/TIP60 co-activator complex, a fusion of the yeast SWR1 and NuA4 complexes, both incorporates the histone variant H2A.Z into nucleosomes and acetylates histones H4/H2A/H2A.Z to play crucial roles regulating gene expression and maintaining genome stability. Our cryo-EM studies show that within the NuA4/TIP60 complex, the EP400 subunit serves as an architectural scaffold holding the different functional modules in specific positions and giving rise to a novel arrangement of the ARP module. EP400 interacts with the TRRAP subunit using a footprint that overlaps with that of the SAGA acetyltransferase complex, thereby preventing the formation of a hybrid complex. Loss of the TRRAP subunit leads to mislocalization of NuA4/TIP60, resulting in the redistribution of H2A.Z and its acetylation across the genome,emphasizing the dual functionality of NuA4/TIP60 as a single macromolecular assembly.

2024-08-08 | PXD053207 | Pride

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