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A low-complexity domain of Tet3 dioxygenase shields the oocyte methylome from oxidative erosion [BiSulfite-seq]

ABSTRACT: A low-complexity domain of Tet3 dioxygenase shields the oocyte methylome from oxidative erosion [BiSulfite-seq]

PROVIDER: PRJNA922209 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR23030721_1.fastq.gz	Fastqsanger.gz
	SRR23030721_2.fastq.gz	Fastqsanger.gz
	SRR23030722_1.fastq.gz	Fastqsanger.gz
	SRR23030722_2.fastq.gz	Fastqsanger.gz
	SRR23030723_1.fastq.gz	Fastqsanger.gz

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A low-complexity domain of Tet3 dioxygenase shields the oocyte methylome from oxidative erosion

Project description:A low-complexity domain of Tet3 dioxygenase shields the oocyte methylome from oxidative erosion

| PRJNA922212 | ENA

A low-complexity domain of Tet3 dioxygenase shields the oocyte methylome from oxidative erosion [RNA-seq]

Project description:Dynamic DNA methylation and demethylation regulate gene expression during development. While DNA methyltransferases (DNMTs) establish and maintain cytosine methylation patterns, Ten-eleven translocation (Tet) dioxygenases catalyze sequential oxidation of 5-methylcytosine (5mC) to promote demethylation. Target-specific 5mC oxidation requires precise regulation of the Tet enzymatic activity. However, the mechanism underlying their activity control remains largely unexplored. Here we show a large low-complexity domain (LCD), present within the catalytic domain of Tet3, functions to repress the dioxygenase activity. Recombinant LCD-deleted Tet3 exhibits enhanced activity to convert 5mC into oxidized species. Deletion of the Tet3 LCD in mouse oocytes renders 5mC oxidation indiscriminately across the genome, leading to most prominently the derepression of ERVK retrotransposons and upregulation of adjacent genes. The extensive 5mC oxidation is associated with impairments in oocyte development. These findings suggest an intrinsic auto-regulatory mechanism of Tet3 dioxygenase operating to ensure a tight regulation of its enzymatic activity to achieve spatiotemporal specificity of methylome reprogramming during oocyte development.

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A low-complexity domain of Tet3 dioxygenase shields the oocyte methylome from oxidative erosion [BiSulfite-seq]

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A low-complexity domain of Tet3 dioxygenase shields the oocyte methylome from oxidative erosion [ ACE-seq]

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A low-complexity domain of Tet3 dioxygenase shields the oocyte methylome from oxidative erosion [RNA-seq]

Project description:A low-complexity domain of Tet3 dioxygenase shields the oocyte methylome from oxidative erosion [RNA-seq]

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A low-complexity domain of Tet3 dioxygenase shields the oocyte methylome from oxidative erosion [ ACE-seq]

Project description:A low-complexity domain of Tet3 dioxygenase shields the oocyte methylome from oxidative erosion [ ACE-seq]

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A low-complexity domain of Tet3 dioxygenase shields the oocyte methylome from oxidative erosion

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

2023-08-24 | GSE222501 | GEO

PGC7 and TET3 ChIP-seq results

Project description:PGC7 is a primordial germ cell (PGCs)-specific protein involved in epigenetic chromatin reprogramming in the zygote following fertilization. TET3 is a dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming in the zygote following fertilization. PGC7 participates in protection of DNA methylation in the maternal pronucleus by preventing conversion of 5mC to 5hmC by TET3 oxidization subsequent DNA demethylation. Thus we tested the co-localization of PGC7 and TET3 in specific loci by ChIP-seq assays.

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PGC7 and TET3 ChIP-seq results

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An auto-suppression mechanism for Tet dioxygenase protects the mouse genome from oxidative demethylation

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