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High throughput sequncing for YTHDC1 binding RNAs [ChIRP-seq]

ABSTRACT: N6-methyladenoisne (m6A) plays critical roles in many biological processes. However, the function of m6A at the early phase of mammalian development remains poorly understood. Here we show that m6A reader Ythdc1 is required for the proliferation of mouse embryonic stem cells (mESCs) in an m6A-dependent manner and its deletion resets mESCs back to a 2C-like state.

ORGANISM(S): Mus musculus

PROVIDER: GSE154328 | GEO | 2021/01/24

REPOSITORIES: GEO

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High throughput sequencing for YTHDC1 binding RNAs [RNA-seq]

Project description:N6-methyladenoisne (m6A) plays critical roles in many biological processes. However, the function of m6A at the early phase of mammalian development remains poorly understood. Here we show that m6A reader Ythdc1 is required for the proliferation of mouse embryonic stem cells (mESCs) in an m6A-dependent manner and its deletion resets mESCs back to a 2C-like state.

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The RNA m6A reader YTHDC1 silences retrotransposons and guards ES cell identity

Project description:The RNA modification N6-methyladenosine (m6A) has critical roles in many biological processes. However, the function of m6A in the early phase of mammalian development remains poorly understood. Here we show that the m6A reader YT521-B homology-domain-containing protein 1 (YTHDC1) is required for the maintenance of mouse embryonic stem (ES) cells in an m6A-dependent manner, and that its deletion initiates cellular reprogramming to a 2C-like state. Mechanistically, YTHDC1 binds to the transcripts of retrotransposons (such as intracisternal A particles, ERVK and LINE1) in mouse ES cells and its depletion results in the reactivation of these silenced retrotransposons, accompanied by a global decrease in SETDB1-mediated trimethylation at lysine 9 of histone H3 (H3K9me3). We further demonstrate that YTHDC1 and its target m6A RNAs act upstream of SETDB1 to repress retrotransposons and Dux, the master inducer of the two-cell stage (2C)-like program. This study reveals an essential role for m6A RNA and YTHDC1 in chromatin modification and retrotransposon repression. This SuperSeries is composed of the SubSeries listed below.

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Structural basis of YTH domain as m6A reader

Project description:The N6-methyladenosine (m6A) is the most abundant internal modification in almost all eukaryotic messenger RNAs, and is dynamically regulated. Therefore, identification of m6A readers is especially important in determining the cellular function of m6A. YTHDF2 has recently been characterized as the first m6A reader that regulates the cytoplasmic stability of methylated RNA. Here we show that YTHDC1 is a nuclear m6A reader and report the crystal structure of the YTH domain of YTHDC1 bound to m6A-containing RNA. We further determined the structure of another YTH domain, YTHDF1, and found that the YTH domain utilizes a conserved aromatic cage to specifically recognize the methyl group of m6A. Our structural characterizations of the YTHDC1-m6A RNA complex also shed light on the molecular basis for the preferential binding of the GG(m6A)C sequence by YTHDC1 and confirm the YTH domain as a specific m6A RNA reader. PAR-CLIP (Photoactivatable-Ribonucleoside-Enhanced Crosslinking and Immunoprecipitation) was applied to human YTHDC1 protein to identify its binding sites.

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