ArticleThe Journal of biological chemistry2011
Queuosine deficiency in eukaryotes compromises tyrosine production through increased tetrahydrobiopterin oxidation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 85 citations in OpenAlex.
- Selective Chemical Manipulation of Mannosyl- and Galactosyl-Queuosine in tRNAs of Living Cells.Angewandte Chemie (International ed. in English) · 2025Article
- Two microbiome metabolites compete for tRNA modification to impact mammalian cell proliferation and translation quality control.Nature cell biology · 2025Article
- Mammalian Queuosine tRNA Modification Impacts Translation to Enhance Cell Proliferation and MHC-II Expression.Journal of molecular biology · 2025Article
- Queuosine tRNA Modification: Connecting the Microbiome to the Translatome.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Decoding the general role of tRNA queuosine modification in eukaryotes.Scientific reports · 2025Article
- Two riboswitch classes that share a common ligand-binding fold show major differences in the ability to accommodate mutations.Nucleic acids research · 2024Article
- 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
- Queuine ameliorates impaired mitochondrial function caused by mt-tRNAJournal of translational medicine · 2024Article
- A new class of 7-deazaguanine agents targeting autoimmune diseases: dramatic reduction of synovial fibroblast IL-6 production from human rheumatoid arthritis patients and improved performance against murine experimental autoimmune encephalomyelitis.RSC medicinal chemistry · 2024Article
- Translational response to mitochondrial stresses is orchestrated by tRNA modifications.bioRxiv : the preprint server for biology · 2024Article
- Synthesis and Structure Elucidation of Glutamyl-Queuosine.Journal of the American Chemical Society · 2023Article
- Queuosine-tRNA promotes sex-dependent learning and memory formation by maintaining codon-biased translation elongation speed.The EMBO journal · 2023Article
- Structural basis of Qng1-mediated salvage of the micronutrient queuine from queuosine-5'-monophosphate as the biological substrate.Nucleic acids research · 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
- Association of Gut Microbiota With Metabolism in Rainbow Trout Under Acute Heat Stress.Frontiers in microbiology · 2022Article
- Dynamic queuosine changes in tRNA couple nutrient levels to codon choice in Trypanosoma brucei.Nucleic acids research · 2021Article
- Synthesis and structure elucidation of the human tRNA nucleoside mannosyl-queuosine.Nature communications · 2021Article
- Modifications of the human tRNA anticodon loop and their associations with genetic diseases.Cellular and molecular life sciences : CMLS · 2021Review
- Variations in transfer and ribosomal RNA epitranscriptomic status can adapt eukaryote translation to changing physiological and environmental conditions.RNA biology · 2021Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Queuosine is a modified pyrrolopyrimidine nucleoside found in the anticodon loop of transfer RNA acceptors for the amino acids tyrosine, asparagine, aspartic acid, and histidine. Because it is exclusively synthesized by bacteria, higher eukaryotes must salvage queuosine or its nucleobase queuine from food and the gut microflora. Previously, animals made deficient in queuine died within 18 days of withdrawing tyrosine, a nonessential amino acid, from the diet (Marks, T., and Farkas, W. R. (1997) Biochem. Biophys. Res. Commun. 230, 233-237). Here, we show that human HepG2 cells deficient in queuine and mice made deficient in queuosine-modified transfer RNA, by disruption of the tRNA guanine transglycosylase enzyme, are compromised in their ability to produce tyrosine from phenylalanine. This has similarities to the disease phenylketonuria, which arises from mutation in the enzyme phenylalanine hydroxylase or from a decrease in the supply of its cofactor tetrahydrobiopterin (BH4). Immunoblot and kinetic analysis of liver from tRNA guanine transglycosylase-deficient animals indicates normal expression and activity of phenylalanine hydroxylase. By contrast, BH4 levels are significantly decreased in the plasma, and both plasma and urine show a clear elevation in dihydrobiopterin, an oxidation product of BH4, despite normal activity of the salvage enzyme dihydrofolate reductase. Our data suggest that queuosine modification limits BH4 oxidation in vivo and thereby potentially impacts on numerous physiological processes in eukaryotes.
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