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Next Generation Sequencing Facilitates Quantitative Analysis of mRNA translation efficiency of Wild Type and Mettl3-/- mice

ABSTRACT: Next Generation Sequencing Facilitates Quantitative Analysis of mRNA translation efficiency of Wild Type and Mettl3-/- mice

PROVIDER: PRJNA423188 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR6395814.fastq.gz	Fastqsanger.gz
	SRR6395815.fastq.gz	Fastqsanger.gz
	SRR6395816.fastq.gz	Fastqsanger.gz
	SRR6395817.fastq.gz	Fastqsanger.gz
	SRR7123172.fastq.gz	Fastqsanger.gz

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Next Generation Sequencing Facilitates Quantitative Analysis of mRNA translation efficiency of Wild Type and Mettl3-/- mice

Project description:Considering m6A modification in mRNA was reported to be intensively corelated with RNA metabolism like RNA decay and RNA translation, we wonderd whether deleting Mettl3, the main catalzing enzyme, affect the RNA translation efficiency of mouse dendritic cells.

2019-04-02 | GSE108331 | GEO

METTL3 promotes translation in human cancer cells

Project description:we find METTL3 associates with polyribosomes and promotes translation. METTL3 depletion inhibits translation, and both wild-type and catalytically inactive METTL3 promote translation when tethered to the 3' untranslated region (UTR) of a reporter mRNA. Mechanistically, METTL3 enhances mRNA translation through an interaction with the translation initiation machinery. m6A seq in A549 and H1299 cells, RNA seq in METTL3 knockdown cells

2016-07-03 | E-GEOD-76367 | biostudies-arrayexpress

METTL3 promotes translation in human cancer cells

2016-01-01 | GSE76367 | GEO

mRNA circularization by METTL3-eIF3h enhances translation

Project description:N6-methyladenosine (m6A) modification of mRNA catalyzed by METTL3 is enriched at a subset of stop codons. METTL3 can promote translation but the mechanism and widespread relevance remain unknown. Here we show that METTL3 enhances translation only when tethered to reporter mRNA at sites close to the stop codon supporting a mRNA looping mechanism for ribosome recycling and translational control. Electron microscopy revealed the topology of individual polyribosomes with single METTL3 foci found in close proximity to 5’ cap-binding proteins. We identify a direct physical and functional interaction between METTL3 and the eukaryotic translation initiation factor 3 subunit h (eIF3h). METTL3 promotes translation of a large subset of oncogenic mRNAs, including BRD4 that are also m6A-modified in human primary lung tumors. The METTL3-eIF3h interaction is required for enhanced translation, formation of densely packed polyribosomes, and oncogenic transformation. METTL3 depletion inhibits tumorigenicity and sensitizes lung cancer cells to BRD4 inhibition. These findings uncover a mRNA looping mechanism of translation control and identify METTL3-eIF3h as a potential cancer therapeutic target.

2018-09-21 | GSE117299 | GEO

PABPN1 effect on translation efficiency.

Project description:PABPN1 effect on translation efficiency.

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TBK1-METTL3 axis facilitates antiviral immunity

Project description:TBK1-METTL3 axis facilitates antiviral immunity

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Next Generation Sequencing Facilitates Quantitative Analysis of METTL3 overexpression in THP-1 cells [RNA-seq]

Project description:The goals of this study are to compare the downstream m6A modification changes and transcriptional changes in AML cells with or without METTL3 overexpression.mRNA profiles of METTL3-ovexpressing THP-1 cells and of its negative control cells were generated by RNA-seq and m6A-seq, in triplicate, using Illumina Hiseq 2000

2022-11-02 | GSE211708 | GEO

Next Generation Sequencing Facilitates Quantitative Analysis of METTL3 overexpression in THP-1 cells [m6A-Seq]

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Next Generation Sequencing Facilitates Quantitative Analysis of METTL3 overexpression in THP-1 cells

Project description:Next Generation Sequencing Facilitates Quantitative Analysis of METTL3 overexpression in THP-1 cells

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N6-methyladenosine Modulates Messenger RNA Translation Efficiency

Project description:N6-methyladenosine (m6A) is the most abundant internal messenger (mRNA) modification in mammalian mRNA. This modification is reversible and non-stoichiometric, which potentially adds an additional layer of variety and dynamic control of mRNA metabolism. The m6A-modified mRNA can be selectively recognized by the YTH family “reader” proteins. The preferential binding of m6A-containing mRNA by YTHDF2 is known to reduce the stability of the target transcripts; however, the exact effects of m6A on translation has yet to be elucidated. Here we show that another m6A reader protein, YTHDF1, promotes ribosome loading of its target transcripts. YTHDF1 forms a complex with translation initiation factors to elevate the translation efficiency of its bound mRNA. In a unified mechanism of translation control through m6A, the YTHDF2-mediated decay controls the lifetime of target transcripts; whereas, the YTHDF1-based translation promotion increases the translation efficiency to ensure effective protein production from relatively short-lived transcripts that are marked by m6A. PAR-CLIP and RIP was used to identify YTHDF1 binding sites followed by ribosome profling and RNA seq to assess the consequences of YTHDF1 siRNA knock-down

2015-06-09 | E-GEOD-63591 | biostudies-arrayexpress

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