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Cancer associated mutants of eIF1A impair Rps3/Rps10 binding and enhance scanning of cell cycle genes [Ribo-Seq]

ABSTRACT: Cancer associated mutants of eIF1A impair Rps3/Rps10 binding and enhance scanning of cell cycle genes [Ribo-Seq]

PROVIDER: PRJNA480786 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR7513745.fastq.gz	Fastqsanger.gz
	SRR7513746.fastq.gz	Fastqsanger.gz
	SRR7513747.fastq.gz	Fastqsanger.gz
	SRR7513748.fastq.gz	Fastqsanger.gz

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Cancer associated mutants of eIF1A impair Rps3/Rps10 binding and enhance scanning of cell cycle genes

Project description:Cancer associated mutants of eIF1A impair Rps3/Rps10 binding and enhance scanning of cell cycle genes

| PRJNA480783 | ENA

Cancer associated mutants of eIF1A impair Rps3/Rps10 binding and enhance scanning of cell cycle genes [Mars-seq]

Project description:Cancer associated mutants of eIF1A impair Rps3/Rps10 binding and enhance scanning of cell cycle genes [Mars-seq]

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Cancer associated mutants of eIF1A impair Rps3/Rps10 binding and enhance scanning of cell cycle genes [Ribo-Seq]

Project description:The Ribo-seq analysis demonstrated that eIF1A is predominantly essential for translation of genes with long 5'UTR genes including cell proliferation and cell cycle progression genes. eIF1A depletion causes broad stimulation of initiation in 5’UTRs at near-cognate AUG codons that diminshes the translation initiation fidelity

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Cancer associated mutants of eIF1A impair Rps3/Rps10 binding and enhance scanning of cell cycle genes [Mars-seq]

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Project description:RPS3, a universal core component of the 40S ribosomal subunit, interacts with mRNA at the entry channel. Whether RPS3 mRNA-binding contributes to specific mRNA translation and ribosome specialization in mammalian cells is unknown. Here we mutated RPS3 mRNA-contacting residues R116, R146 and K148 and report their impact on cellular and viral translation. R116D weakened cap-proximal initiation and promoted leaky scanning, while R146D had the opposite effect. Additionally, R146D and K148D displayed contrasting effects on start-codon fidelity. Translatome analysis uncovered common differentially translated genes of which the downregulated set bears long 5’UTR and weak AUG context, suggesting a stabilizing role during scanning and AUG selection. We identified an RPS3-dependent regulatory sequence (RPS3RS) in the sub-genomic 5’UTR of SARS-CoV-2 consisting of a CUG initiation codon and a downstream element that is also the viral transcription regulatory sequence (TRS). Furthermore, RPS3 mRNA-binding residues were essential for SARS-CoV-2 NSP1-mediated inhibition of host translation and for its ribosomal binding. Intriguingly, NSP1-induced mRNA degradation was also reduced in R116D cells, indicating that mRNA decay occurs in the ribosome context. Thus, RPS3 mRNA-binding residues have multiple translation regulatory functions and are exploited by SARS-CoV-2 in various ways to influence host and viral mRNA translation and stability.

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Cleavage mapping in rps3

Project description:Mapping 3'ends of mRNAs from a reporter subject to no-go decay in an rps3 mutant background.

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Cleavage mapping in rps3

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Project description:Angiotensin II (Ang II) treatment contributes to hypertrophic growth and mitochondrial dysfunction in hiPSC-derived cardiomyocytes. Here, we report enhanced RPS3 phosphorylation at serine 149 in nuclear compartment and abnormal mitochondrial biogenesis during Ang II incubation. Furthermore, RPS3 S149 mutation attenuated Ang II induced cardiomyocyte hypertrophy and improved mitochondrial biogenesis and dysfunction. Mechanistically, RPS3 Ser149 mutation promoted mitochondrial RNA stabilization and blunt Ang II induced mitochodnrial RNA alternative splicing for degradation, by which RPS3 dephosphorylation restored mitochondrial complex assembly in cardiomyocytes.

2023-07-30 | GSE238123 | GEO

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