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Perturbation of the OGT-TET1 interaction in mouse embryonic stem cells (RNA-Seq)

ABSTRACT: Perturbation of the OGT-TET1 interaction in mouse embryonic stem cells (RNA-Seq)

PROVIDER: PRJNA431358 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR7807380.fastq.gz	Fastqsanger.gz
	SRR7807381.fastq.gz	Fastqsanger.gz
	SRR7807382.fastq.gz	Fastqsanger.gz
	SRR7807375.fastq.gz	Fastqsanger.gz
	SRR7807376.fastq.gz	Fastqsanger.gz

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Perturbation of the OGT-TET1 interaction in mouse embryonic stem cells (WGBS)

Project description:Whole genome bisulfite sequencing of wild type embryonic stem cells and cells bearing a mutation that perturbs the OGT-TET1 interaction

2018-10-29 | GSE119665 | GEO

Perturbation of the OGT-TET1 interaction in mouse embryonic stem cells

Project description:Perturbation of the OGT-TET1 interaction in mouse embryonic stem cells

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Perturbation of the OGT-TET1 interaction in mouse embryonic stem cells (RNA-Seq)

Project description:RNA-seq of wild type embryonic stem cells and cells bearing a mutation that perturbs the OGT-TET1 interaction

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Perturbation of the OGT-TET1 interaction in mouse embryonic stem cells (WGBS)

Project description:Perturbation of the OGT-TET1 interaction in mouse embryonic stem cells (WGBS)

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OGT binds a conserved C-terminal domain of TET1 to regulate TET1 activity and function in development

Project description:TET enzymes convert 5-methylcytosine to 5-hydroxymethylcytosine and higher oxidized derivatives. TETs stably associate with and are post-translationally modified by the nutrient-sensing enzyme OGT, suggesting a connection between metabolism and the epigenome. Here, we show for the first time that modification by OGT enhances TET1 activity in vitro. We identify a a domain of TET1 domain that is responsible necessary and sufficient for binding to OGT and report a point mutation that disrupts the TET1-OGT interaction. We show that the TET1-OGTthis interaction is necessary for TET1 to rescue hematopoetic stem cell production in tet mutant zebrafish embryos, suggesting that OGT promotes TET1’s function during development. Finally, we show that disrupting the TET1-OGT interaction in mouse embryonic stem cells changes the abundance of TET-containing high molecular weight complexesTET2 and 5-methylcytosine, which is accompanied by alterations in gene expression and causes widespread gene expression changes. These results link metabolism and epigenetic control, which may be relevant to the developmental and disease processes regulated by these two enzymes.

2018-11-02 | GSE119500 | GEO

Perturbation of the OGT-TET1 interaction in mouse embryonic stem cells

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

2018-10-29 | GSE119666 | GEO

OGT, H2B S112GlcNAc, TET2 ChIP-seq results

Project description:TET2 directly interacts with OGT, which is important for the chromatin association of OGT in vivo. Although this specific interaction does not regulate the enzymatic activity of TET2, it facilitates OGT-dependent histone O-GlcNAcylation. Moreover, OGT associates with TET2 at transcription starting sites (TSS). Down-regulation of TET2 reduces the amount of H2B S112 GlcNAc marks in vivo, which are associated with gene transcription regulation. We found that OGT interacts with TET2 tightly. Using ChIP-seq with specific antibodies, we tested the co-localization of TET2 and OGT in genome level.

2012-12-11 | E-GEOD-41720 | biostudies-arrayexpress

TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS

Project description:TET proteins convert 5-methylcytosine to 5-hydroxymethylcytosine, an emerging dynamic epigenetic state of DNA that can influence transcription. Evidence has linked TET1 function to epigenetic repression complexes, yet mechanistic information, especially for the TET2 and TET3 proteins, remains limited. Here, we show a direct interaction of TET2 and TET3 with O-GlcNAc transferase (OGT). OGT does not appear to influence hmC activity, rather TET2 and TET3 promote OGT activity. TET2/3-OGT co-localize on chromatin at active promoters enriched for H3K4me3 and reduction of either TET2/3 or OGT activity results in a direct decrease in H3K4me3 and concomitant decreased transcription. Further, we show that Host Cell Factor 1 (HCF1), a component of the H3K4 methyltransferase SET1/COMPASS complex, is a specific GlcNAcylation target of TET2/3-OGT, and modification of HCF1 is important for the integrity of SET1/COMPASS. Additionally, we find both TET proteins and OGT activity promote binding of the SET1/COMPASS H3K4 methyltransferase, SETD1A, to chromatin. Finally, studies in Tet2 knockout mouse bone marrow tissue extend and support the data as decreases are observed of global GlcNAcylation and also of H3K4me3, notably at several key regulators of haematopoiesis. Together, our results unveil a step-wise model, involving TET-OGT interactions, promotion of GlcNAcylation, and influence on H3K4me3 via SET1/COMPASS, highlighting a novel means by which TETs may induce transcriptional activation. ChIP-Seq experiments were performed on Illumina HiScanSQ sequencer in wild-type HEK293T cells for H3K4me3 histone marks, O-GlcNAc and HCF1, for HT-TET2, HT-TET3 and HT-OGT in HEK293T cells overexpressing those three fusion proteins and in TET2 Kd HEK293T cells for H3K4me3 histone marks. ChIP-Seqs were also performed in mouse bone marrow tissues for H3K4me3 histone marks, O-GlcNAc, endogenous Tet2 and in Tet2 Ko bone marrow tissues for H3K4me3 histone marks.

2013-02-07 | E-GEOD-36620 | biostudies-arrayexpress

TET1 interactome by SILAC IP-MS in mouse ESCs

Project description:TET1 maintains hypomethylation at bivalent promoters through its catalytic activity in embryonic stem cells (ESCs). However, whether and how TET1 exerts catalytic activity-independent functions in regulating bivalent genes is not well understood. Therefore, we mapped the TET1 interactome in mouse ESCs using a SILAC IP-MS proteomics approach.

2022-06-10 | PXD033587 | Pride

OGT binds a conserved C-terminal domain of TET1 to regulate TET1 activity and function in development

Project description:OGT binds a conserved C-terminal domain of TET1 to regulate TET1 activity and function in development

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