ArticleNature communications2014
Double-sieving-defective aminoacyl-tRNA synthetase causes protein mistranslation and affects cellular physiology and development.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 75 citations in OpenAlex.
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- Mistranslating tRNA variants impact the proteome and phosphoproteome ofbioRxiv : the preprint server for biology · 2025Article
- Lysyl-tRNA synthetase orchestrates translation and hormone signaling during reproduction in Aedes aegypti mosquitoes.Communications biology · 2025Article
- Yeast models for Charcot-Marie-Tooth disease-causing aminoacyl-tRNA synthetase alleles reveal the cellular basis of disease.IUBMB life · 2025Review
- Characterization of a novel heterozygous variant in the histidyl-tRNA synthetase gene associated with Charcot-Marie-Tooth disease type 2W.IUBMB life · 2024Article
- Article
- Mistranslating tRNA variants have anticodon- and sex-specific impacts on Drosophila melanogaster.G3 (Bethesda, Md.) · 2024Article
- Impact of tRNA-induced proline-to-serine mistranslation on the transcriptome of Drosophila melanogaster.G3 (Bethesda, Md.) · 2024Article
- Mistranslating tRNA variants have anticodon- and sex-specific impacts onbioRxiv : the preprint server for biology · 2024Article
- Interplay between mistranslation and oxidative stress inArhiv za higijenu rada i toksikologiju · 2024Article
- Impact of tRNA-induced proline-to-serine mistranslation on the transcriptome ofbioRxiv : the preprint server for biology · 2024Article
- The role of tRNA identity elements in aminoacyl-tRNA editing.Frontiers in microbiology · 2024Review
- Phenylalanine-tRNA aminoacylation is compromised by ALS/FTD-associated C9orf72 C4G2 repeat RNA.Nature communications · 2023Article
- Structural basis of tRNAPro acceptor stem recognition by a bacterial trans-editing domain.Nucleic acids research · 2023Article
- Article
- Recessive aminoacyl-tRNA synthetase disorders: lessons learned fromFrontiers in neuroscience · 2023Review
- A novel mistranslating tRNA model in Drosophila melanogaster has diverse, sexually dimorphic effects.G3 (Bethesda, Md.) · 2022Article
- α-Phenylalanyl tRNA synthetase competes with Notch signaling through its N-terminal domain.PLoS genetics · 2022Article
- Formation and persistence of polyglutamine aggregates in mistranslating cells.Nucleic acids research · 2021Article
- Overview of Metabolomic Analysis and the Integration with Multi-Omics for Economic Traits in Cattle.Metabolites · 2021Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aminoacyl-tRNA synthetases (aaRSs) constitute a family of ubiquitously expressed essential enzymes that ligate amino acids to their cognate tRNAs for protein synthesis. Recently, aaRS mutations have been linked to various human diseases; however, how these mutations lead to diseases has remained unclear. In order to address the importance of aminoacylation fidelity in multicellular organisms, we generated an amino-acid double-sieving model in Drosophila melanogaster using phenylalanyl-tRNA synthetase (PheRS). Double-sieving-defective mutations dramatically misacylate non-cognate Tyr, induce protein mistranslation and cause endoplasmic reticulum stress in flies. Mutant adults exhibit many defects, including loss of neuronal cells, impaired locomotive performance, shortened lifespan and smaller organ size. At the cellular level, the mutations reduce cell proliferation and promote cell death. Our results also reveal the particular importance of the first amino-acid recognition sieve. Overall, these findings provide new mechanistic insights into how malfunctioning of aaRSs can cause diseases.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.