Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Identification of mecciRNAs and their roles in the mitochondrial entry of proteins

ABSTRACT: Identification of mecciRNAs and their roles in the mitochondrial entry of proteins

PROVIDER: PRJNA602675 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR10951070_1.fastq.gz	Fastqsanger.gz
	SRR10951070_2.fastq.gz	Fastqsanger.gz
	SRR10951071_1.fastq.gz	Fastqsanger.gz
	SRR10951071_2.fastq.gz	Fastqsanger.gz
	SRR10951072_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 24

Similar Datasets

Identification of mecciRNAs and their roles in the mitochondrial entry of proteins

Project description:To identify mitochondrial RNAs, we isolated mitochondria and performed RNA sequencing. Differential expression of mRNAs and circRNAs were then analyzed.

2020-01-23 | GSE144063 | GEO

Identification of mitochondrial RNAs [II]

Project description:Identification of mitochondrial RNAs [II]

| PRJNA987585 | ENA

Identification of mitochondrial RNAs [1]

Project description:Identification of mitochondrial RNAs [1]

| PRJNA986504 | ENA

MHC class II proteins mediate cross-species entry of bat influenza viruses

Project description:MHC class II proteins mediate cross-species entry of bat influenza viruses

| PRJNA803440 | ENA

mtran-Transcriptome analysis of mutants in uncharacterised mitochondrial proteins

Project description:ngs2021_04_mac-mtran-Assessment of the impact of loss-of-function of poorly characterised mitochondrial proteins on the nuclear and organellar transcriptome - Transcriptome analysis of mutants in uncharacterised mitochondrial proteins

2023-09-03 | GSE186586 | GEO

Profiling of mRNA localization of nuclear-encoded mitochondrial proteins in zebrafish.

Project description:Current evidence suggests that nuclear-encoded mitochondrial proteins can be locally translated at the mitochondrial surface and co-translationally or post-translationally imported into mitochondria. mRNA localization on the mitochondrial membrane, a prerequisite for localized translation, remains uncharacterized in higher eukaryotic organisms. We employed fractionation-sequencing to profile mitochondria-associated mRNAs in zebrafish larvae. Our transcriptome-wide analysis reveals the localization of mRNAs of only 12% of the nuclear-encoded mitochondrial proteins to the mitochondrial surface, which suggests that post-translational import is the dominant mode of protein import to mitochondria. Additionally, the mRNAs which were localized to the mitochondrial membrane consisted mostly of those encoding proteins involved in mitochondrial dynamics, suggesting their site-specific translation. Finally, we show that the loss of function of the MIA pathway responsible for the post-translational import of a subclass of mitochondrial proteins, triggers mitochondrial localization of mRNAs encoding proteins that are imported to mitochondria via other pathways. Thus, our study suggests that mRNA targeting and localized translation could be relevant in higher eukaryotes to combat stress conditions affecting mitochondrial biogenesis in general.

2023-10-28 | GSE160355 | GEO

mtran-Transcriptome analysis of mutants in uncharacterised mitochondrial proteins

Project description:mtran-Transcriptome analysis of mutants in uncharacterised mitochondrial proteins

| PRJNA774654 | ENA

Mitochondrial Proteostatic Stress Induces Aggrephagy to Triage Unimported Proteins

Project description:Mitochondrial Proteostatic Stress Induces Aggrephagy to Triage Unimported Proteins

| PRJNA427882 | ENA

The FASTK family proteins are master regulators in mitochondrial RNA processing

Project description:Investigation of roles of the FASTK protein family in non-canonical mitochondrial RNA processing

2021-10-19 | GSE156556 | GEO

Targeting and Plasticity of Mitochondrial Proteins Revealed by Proximity-Specific Ribosome Profiling

Project description:Nearly all mitochondrial proteins are nuclear-encoded and are targeted to their mitochondrial destination from the cytosol. Here, we used proximity-specific ribosome profiling to comprehensively measure translation at the mitochondrial surface in yeast. The majority of inner membrane proteins were co-translationally targeted to mitochondria, reminiscent of proteins entering the endoplasmic reticulum (ER). Comparison between mitochondrial and ER localization demonstrated that the vast majority of proteins were targeted to a specific organelle. A prominent exception was the fumarate reductase Osm1, known to reside in mitochondria. We identified a conserved ER isoform of Osm1, which contributes to the oxidative protein folding capacity of the organelle. This dual localization was enabled by alternative translation initiation sites encoding distinct targeting signals. These findings highlight the exquisite in vivo specificity of organellar targeting mechanisms.

2014-11-10 | GSE61011 | 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