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MetabolomicsMultiple modes of interfering with the activity of Plasmodium falciparum cytoplasmic isoleucyl-tRNA synthetase illustrate the enzyme is a promising antimalarial target.
Not available
ORGANISM(S): Plasmodium falciparum 
ST002078 | MetabolomicsWorkbench
ProteomicsOn the mechanism and origin of isoleucyl-tRNA synthetase editing against norvaline
Aminoacyl-tRNA synthetases (aaRSs), the enzymes responsible for coupling tRNAs to their cognate amino acids, minimize translational errors by intrinsic hydrolytic editing. Here, we compared the propensity of norvaline (Nva), a linear amino acid not coded for protein synthesis, to the proteinogenic, ...
ORGANISM(S): Escherichia coli 
2019-01-28 | PXD011051 | Pride
Isoleucyl-trna synthetase E. coli Mistranslation 
TranscriptomicsGlobal analysis of the Staphylococcus aureus response to mupirocin
In the present study we analyzed the response of S. aureus to mupirocin, the drug of choice for nasal decolonization of S. aureus. Mupirocin selectively inhibits the bacterial isoleucyl-tRNA synthetase (IleRSs) leading to the accumulation of uncharged isoleucyl-tRNA and hence (p)ppGpp. The latter is...
ORGANISM(S): Staphylococcus aureus 
2012-01-23 | E-GEOD-30743 | biostudies-arrayexpress
ProteomicsIsoleucyl-tRNA synthetase interactome
Aminoacyl-tRNA synthetases are key enzymes in protein synthesis, as they catalyze the attachment of amino acids to their designated, cognate tRNAs. As such, mutations in aminoacyl-tRNA synthetases are associated with severe diseases, such as neurodevelopmental disorders. Many of these mutations fall...
ORGANISM(S): Homo sapiens (Human) 
2026-03-02 | PXD067475 | Pride
Trna Interactome 
ProteomicsPriestia megaterium response to mupirocin treatment
Isoleucyl-tRNA synthetase (IleRS) is an essential enzyme that covalently couples isoleucine to the corresponding tRNA. Bacterial IleRSs group in two clades, ileS1 and ileS2, the latter bringing resistance to the natural antibiotic mupirocin. Generally, bacteria rely on either ileS1 or ileS2 as a sta...
ORGANISM(S): Priestia Megaterium Nbrc 15308 = Atcc 14581 
2022-08-28 | PXD032256 | JPOST Repository
ProteomicsNeutralization mechanism of a HipA-like toxin targeting isoleucyl-tRNA synthetase
HipAB is a type II toxin-antitoxin (TA) system that targets and inactivates specific aminoacyl-tRNA synthetases in response to various stresses. While the molecular targets and neutralization mechanisms of several HipAB-like TA systems have been well characterized, their structural and functional di...
ORGANISM(S): Escherichia Coli K-12 
2025-04-11 | PXD062828 |
ProteomicsResiliance and proteome response of Escherichia coli to high levels of isoleucine mistranslation
Correct pairing of amino acids and tRNA is prerequisite for correct translation of genetic information during protein biosynthesis. Here, we present effects of proteome-wide isoleucine mistranslation in Escherichia coli induced by editing-defective isoleucyl-tRNA synthetase (IleRS). Two types of mis...
ORGANISM(S): Escherichia Coli 
2024-02-26 | PXD041341 | JPOST Repository
UnknownThe catalytic flexibility of tRNAIle-lysidine synthetase can generate alternative tRNA substrates for isoleucyl-tRNA synthetase.
Not available
S-EPMC2665086 | biostudies-literature
GenomicsA disease-causing Isoleucyl-tRNA synthetase variant leads to altered protein complex formation and cellular stress response
A disease-causing Isoleucyl-tRNA synthetase variant leads to altered protein complex formation and cellular stress response
PRJNA1398246 | ENA
UnknownInhibition of isoleucyl-tRNA synthetase as a potential treatment for human African Trypanosomiasis.
Not available
S-EPMC3656282 | biostudies-literature
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