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7SL RNA and SRP orchestrate a global cellular response to acute thermal stress [RNA-seq]

ABSTRACT: 7SL RNA and SRP orchestrate a global cellular response to acute thermal stress [RNA-seq]

PROVIDER: PRJNA1017529 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR26065440_1.fastq.gz	Fastqsanger.gz
	SRR26065440_2.fastq.gz	Fastqsanger.gz
	SRR26065441_1.fastq.gz	Fastqsanger.gz
	SRR26065441_2.fastq.gz	Fastqsanger.gz
	SRR26065442_1.fastq.gz	Fastqsanger.gz

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7SL RNA and SRP orchestrate a global cellular response to acute thermal stress [RNA-seq]

Project description:Non-coding 7SL RNA is an ancestor to mammalian Alu and B1 SINE RNAs and is thought to function exclusively within the Signal Recognition Particle (SRP), aiding in the translocation of secretory proteins into the endoplasmic reticulum for export. Here, we discover a surprising new function unrelated to protein secretion. Under acute heat shock, 7SL and SRP together selectively arrest cellular transcription and translation machineries as a crucial early response to stress. Under thermal stress, 7SL is upregulated, localizes to the nucleus, and binds to target genes repressed by heat shock. Concurrently, in the cytosol, SRP binds to ribosomes and inhibits new protein synthesis. Translational suppression occurs independently of the signal peptide and is abrogated by depleting SRP. Intriguingly, translation inhibition extends to the mitochondria, as nuclear-encoded mitochondrial genes are enriched among SRP targets. Thus, apart from its role in protein export, 7SL/SRP orchestrates a global response to acute stress that encompasses the nucleus, cytosol, and mitochondria across transcription and translation.

2024-12-29 | GSE243284 | GEO

7SL RNA and SRP orchestrate a global cellular response to acute thermal stress [CHART-seq]

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7SL RNA and SRP orchestrate a global cellular response to acute thermal stress

Project description:7SL RNA and SRP orchestrate a global cellular response to acute thermal stress

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7SL RNA and SRP orchestrate a global cellular response to acute thermal stress [CHART-seq]

Project description:7SL RNA and SRP orchestrate a global cellular response to acute thermal stress [CHART-seq]

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7SL RNA and SRP orchestrate a global cellular response to acute thermal stress [Ribo-seq]

Project description:7SL RNA and SRP orchestrate a global cellular response to acute thermal stress [Ribo-seq]

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7SL RNA and SRP orchestrate a global cellular response to acute thermal stress

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

2024-12-27 | GSE243286 | GEO

7SL RNA and signal recognition particle orchestrate a global cellular response to acute thermal stress.

Project description:Non-coding 7SL RNA is an ancestor to mammalian Alu and B1 SINE RNAs and is thought to function exclusively within the Signal Recognition Particle (SRP), aiding in the translocation of secretory proteins into the endoplasmic reticulum for export. Here, we discover a function of 7SL/SRP unrelated to protein secretion. Under acute heat shock, 7SL and SRP together selectively arrest cellular transcription and translation machineries during early response to stress. Under thermal stress, 7SL is upregulated, accumulates in the nucleus, and binds to target genes repressed by heat shock. Concurrently, in the cytosol, SRP binds to ribosomes and inhibits new protein synthesis. Translational suppression occurs independently of the signal peptide and is abrogated by depleting SRP. Translation inhibition extends to the mitochondria, as nuclear-encoded genes with mitochondrial functions are enriched among SRP targets. Thus, apart from its role in protein export, 7SL/SRP orchestrates a global response to acute stress that encompasses the nucleus, cytosol, and mitochondria across transcription and translation.

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Cotranslational signal independent SRP preloading during membrane targeting

Project description:Cotranslational targeting into the endoplasmic reticulum (ER) by the Signal Recognition Particle (SRP) is a key event determining polypeptide fate in eukaryotic cells. Here, we globally define the principles and mechanisms of SRP binding and ER targeting in vivo. Cotranslational targeting through SRP is the dominant route into the ER for all secretory proteins, regardless of targeting signal characteristics. Cytosolic SRP functions in a pioneer translation round that builds a membrane-resident mRNAs pool, explaining how low SRP levels suffice for the secretory load. SRP does not induce an elongation arrest; consequently, kinetic competition between targeting and translation elongation dictates which substrates are translocated post-translationally. Unexpectedly, SRP binds most secretory ribosomal complexes before targeting signals are synthesized. We show non-coding mRNA elements can promote signal-independent SRP pre-recruitment. Our study defines the complex kinetic interplay between elongation and determinants in the polypeptide and mRNA modulating SRP-substrate selection and membrane targeting in vivo. Ribosome profiling (RiboSeq) and RNA-seq of subcellular fractions of ribosomes. Soluble and membrane bound ribosomes are separated by centrifugation, and SRP-bound ribosomes are immunoprecipitated from the soluble fraction. Polysomes and monosomes are separated by sucrose gradient ultracentrifugation.

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