ArticleThe Journal of biological chemistry2009
Queuosine formation in eukaryotic tRNA occurs via a mitochondria-localized heteromeric transglycosylase.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 70 citations in OpenAlex.
- Defective queuosine and i6A/ms2i6A modification of tRNATyr cause frameshifting and protein aggregation.Nucleic acids research · 2026Article
- Gut microbiota dysbiosis in COPD patients increases the level of queuine in the blood serum abnormally enhancing the viability of lung epithelial cells.Frontiers in immunology · 2026Article
- Two microbiome metabolites compete for tRNA modification to impact mammalian cell proliferation and translation quality control.Nature cell biology · 2025Article
- Decoding the Minimal Translation System of the Plasmodium falciparum Apicoplast: Essential tRNA-modifying Enzymes and Their Roles in Organelle Maintenance.Journal of molecular biology · 2025Article
- Queuosine is incorporated into precursor tRNA before splicing.Nature communications · 2025Article
- Comparative Genomics of Chloropicon primus and Chloropicon roscoffensis Provide Insights into the Evolutionary Dynamics and Ecological Success of These Tiny Green Algae in Marine Environments.Genome biology and evolution · 2025Article
- Queuosine tRNA Modification: Connecting the Microbiome to the Translatome.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Development, validation and application of an LC-MS/MS method quantifying free forms of the micronutrients queuine and queuosine in human plasma using a surrogate matrix approach.Analytical and bioanalytical chemistry · 2024Article
- Detection of queuosine and queuosine precursors in tRNAs by direct RNA sequencing.Nucleic acids research · 2023Article
- Queuosine-tRNA promotes sex-dependent learning and memory formation by maintaining codon-biased translation elongation speed.The EMBO journal · 2023Article
- Functional integration of a semi-synthetic azido-queuosine derivative into translation and a tRNA modification circuit.Nucleic acids research · 2022Article
- The importance of RNA modifications: From cells to muscle physiology.Wiley interdisciplinary reviews. RNA · 2022Review
- tRNA modification dynamics from individual organisms to metaepitranscriptomics of microbiomes.Molecular cell · 2022Review
- Are Metabolites From the Gut Microbiota Capable of Regulating Epigenetic Mechanisms in the Human ParasiteFrontiers in cell and developmental biology · 2022Review
- Human transfer RNA modopathies: diseases caused by aberrations in transfer RNA modifications.The FEBS journal · 2021Review
- Mitochondrial noncoding RNAs: new wine in an old bottle.RNA biology · 2021Review
- Variations in transfer and ribosomal RNA epitranscriptomic status can adapt eukaryote translation to changing physiological and environmental conditions.RNA biology · 2021Review
- Article
- The expanding world of tRNA modifications and their disease relevance.Nature reviews. Molecular cell biology · 2021Review
- The human tRNA-guanine transglycosylase displays promiscuous nucleobase preference but strict tRNA specificity.Nucleic acids research · 2021Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
tRNA guanine transglycosylase (TGT) enzymes are responsible for the formation of queuosine in the anticodon loop (position 34) of tRNA(Asp), tRNA(Asn), tRNA(His), and tRNA(Tyr); an almost universal event in eubacterial and eukaryotic species. Despite extensive characterization of the eubacterial TGT the eukaryotic activity has remained undefined. Our search of mouse EST and cDNA data bases identified a homologue of the Escherichia coli TGT and three spliced variants of the queuine tRNA guanine transglycosylase domain containing 1 (QTRTD1) gene. QTRTD1 variant_1 (Qv1) was found to be the predominant adult form. Functional cooperativity of TGT and Qv1 was suggested by their coordinate mRNA expression in Northern blots and from their association in vivo by immunoprecipitation. Neither TGT nor Qv1 alone could complement a tgt mutation in E. coli. However, transglycosylase activity could be obtained when the proteins were combined in vitro. Confocal and immunoblot analysis suggest that TGT weakly interacts with the outer mitochondrial membrane possibly through association with Qv1, which was found to be stably associated with the organelle.
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Registered trials
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.