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

ABSTRACT: 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.

ORGANISM(S): Homo sapiens

PROVIDER: GSE110405 | GEO | 2019/12/01

REPOSITORIES: GEO

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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.

2019-12-01 | GSE110406 | GEO

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

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

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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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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

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 [ChIP-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.

2023-12-24 | GSE245116 | GEO

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

2023-12-24 | GSE245115 | GEO

ChIP-seq of TIP60 complex

Project description:Genome-wide mapping of TIP60 complex subunits in K562 cells. The objectives of this study are to describe TIP60 genome wide localization, confirm MBTD1 co-localization with already known unique subunits and observe the impact of MBTD1 on TIP60 complex targeting to chromatin. The TIP60 acetyltransferase complex is a key regulator of genome expression and stability. Here, we identified MBTD1 as a new stable subunit of the complex and revealed interesting insights about TIP60 function during the repair of DNA double strand breaks. MBTD1 binds H4K20me1/2, helping TIP60 association to specific promoters but also the DNA repair process by homologous recombination. While pro-end joining factor 53BP1 engages chromatin through simultaneous binding of H4K20me2 and H2AK15ub, TIP60 regulates the resolution of 53BP1 foci after DNA damage through a related bivalent mechanism. MBTD1 competes with 53BP1 for the H4K20me2 mark, affecting its retention at the break cooperatively with H4 acetylation by TIP60. In addition, we show that H2AK15ub deposition by RNF168 inhibits chromatin acetylation by TIP60, whereas H2AK15 can also be acetylated by TIP60 in vivo, therefore blocking its ubiquitylation. Altogether, these results uncover an intricate mechanism orchestrated by the TIP60 complex to regulate 53BP1-dependent repair pathway selection, through incompatible bivalent binding/action on chromatin.

2016-04-30 | GSE69645 | GEO

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