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TIP60-dependent acetylation on H2AZ lysine 7 regulates the transcriptional program for genome stability

ABSTRACT: TIP60-dependent acetylation on H2AZ lysine 7 regulates the transcriptional program for genome stability

PROVIDER: PRJNA433650 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR6703500_1.fastq.gz	Fastqsanger.gz
	SRR6703500_2.fastq.gz	Fastqsanger.gz
	SRR6703501.fastq.gz	Fastqsanger.gz
	SRR6703502.fastq.gz	Fastqsanger.gz
	SRR6703503.fastq.gz	Fastqsanger.gz

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TIP60-dependent acetylation on H2AZ lysine 7 regulates the transcriptional program for genome stability [RNA-seq]

Project description:TIP60 mediated acetylation of H2AZ on gene promoter results in change in transcriptional landscape, and further regulates expression of genes involved in the maintenance of genome stability.

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TIP60-dependent acetylation on H2AZ lysine 7 regulates the transcriptional program for genome stability [ChIP-seq]

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TIP60-dependent acetylation on H2AZ lysine 7 regulates the transcriptional program for genome stability [ChIP-seq]

Project description:TIP60-dependent acetylation on H2AZ lysine 7 regulates the transcriptional program for genome stability [ChIP-seq]

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TIP60-dependent acetylation on H2AZ lysine 7 regulates the transcriptional program for genome stability [RNA-seq]

Project description:TIP60-dependent acetylation on H2AZ lysine 7 regulates the transcriptional program for genome stability [RNA-seq]

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Detection of H2AZ acetylation, total H2AZ, and H4K8 and H4K16 acetylation by CUT&Tag-sequencing

Project description:Detection of H2AZ acetylation, total H2AZ, and H4K8 and H4K16 acetylation by CUT&Tag-sequencing

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Detection of H2AZ acetylation, total H2AZ, and H4K8 and H4K16 acetylation by CUT&Tag-sequencing

Project description:In this study we examined the effects of loss of the MYST histone acetyltransferase TIP60 (KAT5) in mouse embryonic fibroblasts (MEFs), human embryonic kidney cells 293 (HEK293), and human osteosarcoma cells (U2OS) on cell proliferation, BrdU incorporation, cell cycle progression, apoptotic and other forms of cell death, DNA damage, histone acetylation at specific lysine residues and RNA expression levels. This dataset relates to U2OS cells. CUT&Tag was performed on replicate cultures and 100,000 cells per sample, 43,000 human cells each of U2OS with inducible single guide RNA #1 (g1/C9) or inducible single guide RNA #2 (g2/C9) expression and both with constitutive expression of Cas9 enzyme, either treated with doxycycline for 4 days (KO) or untreated (CTL) and 57,000 D. melanogaster cells as a spike-in, in total two replicates of TIP60 deleted cells and two replicates of control cells.

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Role of the Tudor-knot domain of the TIP60 lysine acetyltransferase [RNA-seq]

Project description:The histone lysine acetyltransferase TIP60 is the main enzyme that catalyzes histone H4 acetylation in cells. Domains on TIP60 regulate its enzymatic activity from different aspects. Here we use a CRISPR-Cas9 tiling screen to scan for essential domains on TIP60 protein and found that the Tudor-knot domain is essential for cell survival and intercellular H4 acetylation. We performed in-vitro biochemical assays and demonstrated Tudor-knot domain is not a histone reader. And deficiency of the Tudor-knot domain has mild effects on TIP60 intracellular localization, as well as the TIP60 complex’s constitution. But Tudor-knot deficiency significantly reduces TIP60 HAT activity both in vivo and in vitro. By comparing the catalytic efficiency of nucleosome substrate and histone octamer substrate, as well as TIP60 protein alone or TIP60 complex, we found the nucleosomal structure and other TIP60 complex components are required for Tudor-knot relative HAT activity regulation. We propose that the Tudor-knot domain function to increase nucleosome accessibility. Finally, we show that the Tudor-knot domain is required for TIP60-dependent transcription regulation. Altogether, our study reveals a mechanism that the Tudor-knot domain that regulates TIP60-dependent transcription through the regulation of TIP60 substrate catalytic efficiency.

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Role of the Tudor-knot domain of the TIP60 lysine acetyltransferase [ChIP-seq]

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Lysine acetyltransferase Tip60 is required for hematopoietic stem cells maintenance

Project description:Hematopoietic stem cells (HSC) have the potential to replenish the blood system for the lifetime of the organism. Their two defining properties, self-renewal and differentiation, are tightly regulated by the epigenetic machineries. Here, using conditional gene knockout models, we demonstrate a critical requirement of lysine acetyltransferase 5 (also known as Tip60) for murine HSC maintenance both in the embryonic and adult stages, which depends on its acetyltransferase activity. Genome-wide chromatin and transcriptome profiling revealed that Tip60 co-localizes with c-Myc and that Tip60 deletion suppress the expression of Myc target genes, which are associated with critical biological processes for HSC maintenance, cell-cycle and DNA repair. Notably, acetylated H2A.Z (acH2A.Z) was enriched at the Tip60-bound active chromatin and Tip60 deletion induced a robust reduction in the acH2A.Z / H2A.Z ratio. These results uncover a critical epigenetic regulatory layer for HSC maintenance through Tip60 dependent H2A.Z acetylation to activate Myc target genes.

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TIP60-dependent acetylation on H2AZ lysine 7 regulates the transcriptional program for genome stability

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

2019-12-01 | GSE110407 | GEO