Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Saccharomyces cerevisiae

ABSTRACT: Ribosome profiling study of eIF5A depletion strain

PROVIDER: PRJNA352976 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR5008134.fastq.gz	Fastqsanger.gz
	SRR5008135.fastq.gz	Fastqsanger.gz
	SRR5008136.fastq.gz	Fastqsanger.gz
	SRR5008137.fastq.gz	Fastqsanger.gz
	SRR5008138.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 8

Similar Datasets

Saccharomyces cerevisiae

Project description:Study of ribosome dynamics after eIF5A depletion in budding yeast

| PRJNA356767 | ENA

Ribosome profiling of budding yeast Saccharomyces cerevisiae in eEF3 depleted conditions

Project description:Ribosome profiling (Ribo-Seq) and RNA-Seq analysis of eEF3 depletion in yeast (Saccharomyces cerevisiae). eEF3 depletion was induced by methionine in a modified strain where the native promoter was replaced by methionine repressible MET25 promoter. Conditional depletion enables us to study global effects of an essential gene.

2018-06-30 | E-MTAB-6938 | biostudies-arrayexpress

Saccharomyces cerevisiae

Project description:Ribosome profiling study of rli1 depeletion strain

| PRJNA285458 | ENA

Ribosome profiling study of eIF5A depletion strain

Project description:The eukaryotic translation factor eIF5A, originally identified as an initiation factor, was later shown to promote translation elongation of iterated proline sequences. Using a combination of ribosome profiling and in vitro biochemistry, we report a much broader role for eIF5A in elongation and uncover a substantial function for eIF5A in termination. Ribosome profiling of an eIF5A-depleted strain reveals a global elongation defect, with abundant ribosomes stalling at many sequences, not limited to proline stretches. Our data also show accumulation at stop codons and in the 3’-UTR, suggesting a global defect in termination in the absence of eIF5A. Using an in vitro reconstituted translation system, we find that eIF5A strongly promotes the translation of novel stalling sequences and increases the rate of peptidyl-tRNA hydrolysis more than 17-fold. We conclude that eIF5A functions broadly in elongation and termination, rationalizing its great cellular abundance and essential nature.

2017-04-07 | GSE89704 | GEO

Saccharomyces cerevisiae

Project description:Ribosome profiling study of Dhh1p overexpression and the dhh1 knockout strain using monosome-protected footprints

| PRJNA321151 | ENA

ncRNA termination in Saccharomyces cerevisiae

Project description:Nuclear depletion of the essential transcription termination factor Nrd1 in Saccharomyces cerevisiae was studied using a combination of RNA-Seq, ChIP-Seq of Pol II and PAR-CLIP of Nrd1. The drug rapamycin induces the formation of a ternary complex between a protein of interest, the drug and the small subunit of the ribosome (both proteins are genetically engineered). The small ribosome subunit is transported out of the nucleus. therefore the protein of interest can be depleted from nucleus upon treatment with rapamycin.

2013-11-14 | E-MTAB-1766 | biostudies-arrayexpress

Saccharomyces cerevisiae

Project description:Ribosome profiling of dhh1∆ yeast

| PRJNA348115 | ENA

Saccharomyces cerevisiae

Project description:Ribosome profiling of whi3 mutant yeast

| PRJNA221377 | ENA

Saccharomyces cerevisiae strain:AJY3373

Project description:Saccharomyces cerevisiae ribosome profiling

| PRJNA289465 | ENA

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

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 | GSE132008 | 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