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RNA-seq and ribosome profiling of heat shocked wild type and Mettl14 -/- mouse embryonic stem cells

ABSTRACT: RNA-seq and ribosome profiling of heat shocked wild type and Mettl14 -/- mouse embryonic stem cells

PROVIDER: PRJNA517401 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8494660.fastq.gz	Fastqsanger.gz
	SRR8494670.fastq.gz	Fastqsanger.gz
	SRR8494680.fastq.gz	Fastqsanger.gz
	SRR8494690.fastq.gz	Fastqsanger.gz
	SRR8494700.fastq.gz	Fastqsanger.gz

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Ribosome profiling on heat shocked wild type and Mettl14 -/- mES cells

Project description:Ribosome profiling on heat shocked wild type and Mettl14 -/- mES cells

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Ribosome profiling on heat shocked wild type and Mettl14 -/- mES cells

Project description:Abstract : "A hallmark of the cellular response to environmental stress is the formation of stress granules. Stress granules are RNA-protein assemblies that provide an adaptive response to stress; however, the basis for their formation and how they contribute to the stress response remains incompletely understood. Here we show that the mRNA modification N6-methyladenosine (m6A) is a mark that targets mRNAs to stress granules. We find that m6A mRNAs are highly enriched in stress granules, and this is mediated by m6A-induced liquid-liquid phase separation of the YTHDF family of m6A-binding proteins. These proteins bind poly-methylated m6A mRNAs, causing them to form liquid droplets that partition into stress granules. Moreover, disrupting either m6A or YTHDF proteins prevents stress granule formation." The goal of this experiment is to understand how recruitment of m6A mRNA to stress granules influences the translational response to heat shock. Result: we found that m6A-containing mRNA are preferentially repressed during stress, and that m6A is required for translational recovery after heat shock

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RNA-seq and ribosome profiling of heat shocked wild type and Mettl14 -/- mouse embryonic stem cells

Project description:N6-methyladenosine (m6A) is a dynamic and reversible nucleotide modification in mRNA. m6A alters mRNA fate, but it is unclear why the effects of m6A can vary in different cellular contexts. Here we show that methylated mRNAs are catalysts for liquid-liquid phase separation of the YTHDF family of m6A-binding proteins. RNAs that contain multiple, but not single, m6A residues recruit multiple YTHDF proteins, causing them to undergo a proximity-induced phase separation. YTHDF proteins show liquid-like properties upon binding polymethylated mRNAs in cells, and partition into endogenous phase-separated compartments, such as P-bodies, neuronal RNA granules, and stress granules. The complexes of YTHDF proteins and polymethylated mRNAs are targeted to different compartments depending on the cell context, leading to different effects on m6A mRNAs. These studies reveal a role for nucleotide modifications in regulating phase separation and indicate that the cellular properties of m6A-modified mRNAs can be explained by liquid-liquid phase separation principles.

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