Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Induction of proteasomal activity in mammalian cells by lifespan-extending tRNA synthetase inhibitors

ABSTRACT: Induction of proteasomal activity in mammalian cells by lifespan-extending tRNA synthetase inhibitors

PROVIDER: PRJNA899861 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR22246800_1.fastq.gz	Fastqsanger.gz
	SRR22246800_2.fastq.gz	Fastqsanger.gz
	SRR22246801_1.fastq.gz	Fastqsanger.gz
	SRR22246801_2.fastq.gz	Fastqsanger.gz
	SRR22246802_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 92

Similar Datasets

Induction of proteasomal activity in mammalian cells by lifespan-extending tRNA synthetase inhibitors

Project description:ATF4-dependent differential transcription in response to tRNA synthetase inhibitor treatment in mouse embryonic fibroblasts We performed RNAseq on wild type and ATF4 KO mouse embryonic fibroblasts with and without tRNA synthetase inhibitor as our block design described in JAAA-D-23-00283R1 by Geroscience

2023-09-05 | GSE217634 | GEO

tRNA overexpression rescues peripheral neuropathy caused by mutations in tRNA synthetase

Project description:Heterozygous mutations in six tRNA synthetase genes cause Charcot-Marie-Tooth (CMT) peripheral neuropathy. CMT-mutant glycyl- or tyrosyl-tRNA synthetases inhibit global protein synthesis by an unknown mechanism, independent of aminoacylation activity. We report that tRNAGly overexpression rescues protein synthesis and peripheral neuropathy phenotypes in Drosophila and mouse models of CMT caused by glycyl-tRNA synthetase (GlyRS) mutations (CMT2D). Kinetic experiments revealed that CMT-mutant GlyRS bind tRNAGly, but display markedly slow release rates. This tRNAGly sequestration may deplete the cellular tRNAGly pool, leading to insufficient glycyl-tRNAGly supply to the ribosome and translation deficit.

2021-09-07 | GSE160584 | GEO

McFarland2020 - Synthetase sequestration Model:a combined translation and tRNA charging cycle

Project description:The Synthetase Sequestration Model (SSM) is a simplified translation model that considers explicitly two main steps in the process of tRNA aminoacylation: first, the tRNA is bound by the aminoacyl tRNA synthetase, and in a second step, the amino acid is attached to the tRNA. The tRNA then participates in the translation reaction, becoming deacylated as a result. The tRNA exists in states bound, charged and uncharged. In the bound state, the tRNA is bound to the synthetase but uncharged, i.e., the tRNA is sequestered by the synthetase. The model predicts how the balance between the three different tRNA states (empty, bound and charged) changes depending on aminoacyl tRNA synthetase availability.

2020-02-05 | MODEL2001080005 | BioModels

Growth Optimized Aminoacyl-tRNA Synthetase Levels Prevent Maximal tRNA Charging

Project description:Growth Optimized Aminoacyl-tRNA Synthetase Levels Prevent Maximal tRNA Charging

| PRJNA593256 | ENA

Mouse Liver LC-MS/MS Analysis Following Treatment With Lifespan-Extending Drugs

Project description:Aging manifests as progressive deterioration in cellular and systemic homeostasis, requiring systems-level perspectives to understand the gradual molecular dysregulation of underlying biological processes. Here, we collected data for the analysis of systems-level changes in the molecular regulation of biological processes under multiple lifespan-extending interventions in mice. High-resolution shotgun LC-MS/MS data were collected from liver samples obtained from multiple mouse cohorts treated with different lifespan-extending drugs, and analyzed using reverse phase liquid chromatography on Orbitrap mass spectrometers.

2023-07-25 | PXD035255 | Pride

Transcriptional responses to glutaminyl tRNA synthetase Gln4p depletion in Saccharomyces cerevisiae

Project description:A tet-off strain of Saccharomyces cerevisiae was constructed in which the GLN4 glutamine tRNA synthetase gene was placed under control of a doxycycline-regulated promoter. The transcriptional responses to Gln4p tRNA synthetase depletion were assessed by growth of the strain in the presence, or absence, of doxycycline (1 µg/ml). A control, wild-type strain was similarly treated with doxycycline or left untreated as a reference. Each strain/condition RNA isolation was performed using triplicate independent biological samples A, B and C.

2019-04-01 | GSE126435 | GEO

Chimeric design of Pyrrolysyl-tRNA synthetase/tRNA pairs and canonical synthetase/tRNA pairs for genetic code expansion

Project description:An orthogonal aminoacyl-tRNA synthetase/tRNA pair is a key prerequisite for site-specific incorporation of unnatural amino acids. Due to its high codon suppression efficiency and full orthogonality, the pyrrolysyl-tRNA synthetase/pyrrolysyl-tRNA pair is currently the ideal system for genetic code expansion in both eukaryotes and prokaryotes. There is a pressing need to discover or engineer other fully orthogonal translation systems that allow unnatural amino acids with distinct scaffolds and functionalities to be incorporated into a wide range of living organisms efficiently. Here, through rational chimera design by transplanting the key orthogonal components from the pyrrolysine system, we create multiple chimeric tRNA synthetase/chimeric tRNA pairs, including chimera histidine, phenylalanine, and alanine systems. We further show that these engineered chimeric systems are orthogonal and highly efficient with comparable flexibility to the pyrrolysine system. In addition, the chimera phenylalanine system can incorporate a group of phenylalanine, tyrosine and tryptophan analogues efficiently in both E. coli and mammalian cells. These aromatic amino acids analogous exhibit unique properties and characteristics, including fluorescence, post-translation modification. To our knowledge, most of these molecules have never been shown to be incorporated with fully orthogonal pairs. Therefore, these chimera pairs offer the potential for incorporation of de novo unnatural amino acids into target proteins for a variety of applications.

2020-05-25 | PXD018660 | Pride

tRNA overexpression rescues peripheral neuropathy caused by mutations in tRNA synthetase

Project description:tRNA overexpression rescues peripheral neuropathy caused by mutations in tRNA synthetase

| PRJNA673697 | ENA

RNA sequencing of mouse hepatic response to lifespan-extending interventions

Project description:RNA sequencing of mouse hepatic response to lifespan-extending interventions

| PRJNA544682 | ENA

Lithocholic acid significantly extends the lifespan in Drosophila melanogaster by targeting multiple lifespan-extending pathways

Project description:Lithocholic acid significantly extends the lifespan in Drosophila melanogaster by targeting multiple lifespan-extending pathways

| PRJNA433535 | ENA

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