Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection (CRISPR screen)

ABSTRACT: Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection (CRISPR screen)

PROVIDER: PRJNA545621 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR9165270.fastq.gz	Fastqsanger.gz
	SRR9165280.fastq.gz	Fastqsanger.gz
	SRR9165271.fastq.gz	Fastqsanger.gz
	SRR9165281.fastq.gz	Fastqsanger.gz
	SRR9165272.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 16

Similar Datasets

Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection (CRISPR screen)

Project description:Sequences within 5' untranslated regions (UTRs) dictate the site and efficiency of translation initiation. In this study, an unbiased screen designed to interrogate the 5' UTR-mediated regulation of the growth-promoting gene MYC unexpectedly revealed the ribosomal pause-relief factor eIF5A as a regulator of translation initiation codon selection. Depletion of eIF5A enhanced upstream translation within 5' UTRs across yeast and human transcriptomes, including on the MYC transcript where this resulted in increased production of an N-terminally extended protein. Furthermore, ribosome profiling experiments established that the function of eIF5A as a suppressor of ribosomal pausing at sites of suboptimal peptide bond formation is conserved in human cells. We present evidence that proximal ribosomal pausing on a transcript triggers enhanced usage of upstream suboptimal or non-canonical initiation codons. Thus, we propose that eIF5A functions not only to maintain efficient translation elongation in eukaryotic cells, but also to maintain the fidelity of translation initiation.

2019-12-03 | GSE132009 | GEO

Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection (RNA-sequencing)

2019-12-03 | GSE132008 | GEO

Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection (Ribosome profiling)

2019-12-03 | GSE132007 | GEO

Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection

Project description:Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection

| PRJNA545619 | ENA

Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection (RNA-sequencing)

Project description:Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection (RNA-sequencing)

| PRJNA545624 | ENA

Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection (Ribosome profiling)

Project description:Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection (Ribosome profiling)

| PRJNA545625 | ENA

Suppression of Ribosomal Pausing by eIF5A Is Necessary to Maintain the Fidelity of Start Codon Selection.

Project description:Sequences within 5' UTRs dictate the site and efficiency of translation initiation. In this study, an unbiased screen designed to interrogate the 5' UTR-mediated regulation of the growth-promoting gene MYC unexpectedly revealed the ribosomal pause relief factor eIF5A as a regulator of translation initiation codon selection. Depletion of eIF5A enhances upstream translation within 5' UTRs across yeast and human transcriptomes, including on the MYC transcript, where this results in increased production of an N-terminally extended protein. Furthermore, ribosome profiling experiments established that the function of eIF5A as a suppressor of ribosomal pausing at sites of suboptimal peptide bond formation is conserved in human cells. We present evidence that proximal ribosomal pausing on a transcript triggers enhanced use of upstream suboptimal or non-canonical initiation codons. Thus, we propose that eIF5A functions not only to maintain efficient translation elongation in eukaryotic cells but also to maintain the fidelity of translation initiation.

| S-EPMC6917043 | biostudies-literature

Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection

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

2019-12-03 | GSE132010 | GEO

Start codon-associated ribosomal frameshifting mediates nutrient stress adaptation

Project description:A translating ribosome is typically thought to follow the reading frame defined by the selected start codon. Using super-resolution ribosome profiling, here we report pervasive out-of-frame translation from the start codon. Unlike programmable frameshifting during elongation, start codon-associated ribosome frameshifting (SCARF) stems from the slippage of the initiating ribosome. Using a massively paralleled reporter assay, we uncovered sequence elements acting as SCARF enhancers or repressors, implying that start codon recognition is coupled with reading frame fidelity. This finding explains thousands of mass spectrometry spectra unannotated from human proteome. Mechanistically, we find that the eukaryotic initiation factor 5B (eIF5B) maintains the reading frame fidelity during the transition from initiation to elongation. Intriguingly, amino acid starvation induces SCARF by proteasomal degradation of eIF5B. The stress-induced SCARF products provide a degradative source to mitigate amino acid scarcity during starvation. Our findings illustrate the beneficial effect of divergent translation in nutrient stress adaptation.

2023-03-01 | GSE184825 | GEO

Translational fidelity screens reveal eIF3 as a key regulator of start codon selectivity [RNA-seq]

Project description:To investigate the function eIF3D, eIF1A, eIF4G2, and ZNF324 in near-cognate start codon usage, we established K562, HeLa, and Jurkat cell lines in which each target gene has been knocked down by CRISPRi sgRNAs.

2023-05-05 | GSE207330 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data