ArticleJournal of molecular biology2013
Structural and mechanistic basis for enhanced translational efficiency by 2-thiouridine at the tRNA anticodon wobble position.
Article in Journal of molecular biology, 2013. 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, 78 citations in OpenAlex.
- EnterohemorrhagicmSystems · 2026Article
- Synthesis and Hybridization Properties of RNA Oligomers Containing Biologically Relevant 5-Aminomethyl-2-thiouridines (xnmCurrent medicinal chemistry · 2026Article
- Uridines Modified with Sulfur or Selenium in U-G Wobble Pairs Matter for tRNA Function.Current medicinal chemistry · 2026Review
- Beyond RNA modification: a novel role for tRNA modifying enzyme in oxidative stress response and metabolism.Nucleic acids research · 2025Article
- tRNA modifications as regulators of bacterial virulence and stress responses.PLoS pathogens · 2025Review
- Activation of Caged Functional RNAs by An Oxidative Transformation.Chembiochem : a European journal of chemical biology · 2025Article
- Studies on the Oxidative Damage of the Wobble 5-Methylcarboxymethyl-2-Thiouridine in the tRNA of Eukaryotic Cells with Disturbed Homeostasis of the Antioxidant System.International journal of molecular sciences · 2024Article
- SARS-CoV-2 Displays a Suboptimal Codon Usage Bias for Efficient Translation in Human Cells Diverted by Hijacking the tRNA Epitranscriptome.International journal of molecular sciences · 2024Article
- Anticodon stem-loop tRNA modifications influence codon decoding and frame maintenance during translation.Seminars in cell & developmental biology · 2024Review
- The thiolation of uridine 34 in tRNA, which controls protein translation, depends on a [4Fe-4S] cluster in the archaeum Methanococcus maripaludis.Scientific reports · 2023Article
- Identification of a novel 5-aminomethyl-2-thiouridine methyltransferase in tRNA modification.Nucleic acids research · 2023Article
- Expansion of the genetic code through reassignment of redundant sense codons using fully modified tRNA.Nucleic acids research · 2022Article
- Demystifying mRNA vaccines: an emerging platform at the forefront of cryptic diseases.RNA biology · 2022Review
- Disease-associated mutations in a bifunctional aminoacyl-tRNA synthetase gene elicit the integrated stress response.The Journal of biological chemistry · 2021Article
- Multiplex suppression of four quadruplet codons via tRNA directed evolution.Nature communications · 2021Article
- Loss ofeLife · 2021Article
- TusA Is a Versatile Protein That Links Translation Efficiency to Cell Division in Escherichia coli.Journal of bacteriology · 2021Article
- Comparative tRNA sequencing and RNA mass spectrometry for surveying tRNA modifications.Nature chemical biology · 2020Article
- Naturally occurring modified ribonucleosides.Wiley interdisciplinary reviews. RNA · 2020Review
- Review
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Authors and funding
9 authors at 6 institutions in 1 country.
Funding
Abstract
The 2-thiouridine (s(2)U) at the wobble position of certain bacterial and eukaryotic tRNAs enhances aminoacylation kinetics, assists proper codon-anticodon base pairing at the ribosome A-site, and prevents frameshifting during translation. By mass spectrometry of affinity-purified native Escherichia coli tRNA1(Gln)UUG, we show that the complete modification at the wobble position 34 is 5-carboxyaminomethyl-2-thiouridine (cmnm(5)s(2)U). The crystal structure of E. coli glutaminyl-tRNA synthetase (GlnRS) bound to native tRNA1(Gln) and ATP demonstrates that cmnm(5)s(2)U34 improves the order of a previously unobserved 11-amino-acid surface loop in the distal β-barrel domain of the enzyme and imparts other local rearrangements of nearby amino acids that create a binding pocket for the 2-thio moiety. Together with previously solved structures, these observations explain the degenerate recognition of C34 and modified U34 by GlnRS. Comparative pre-steady-state aminoacylation kinetics of native tRNA1(Gln), synthetic tRNA1(Gln) containing s(2)U34 as sole modification, and unmodified wild-type and mutant tRNA1(Gln) and tRNA2(Gln) transcripts demonstrates that the exocyclic sulfur moiety improves tRNA binding affinity to GlnRS 10-fold compared with the unmodified transcript and that an additional fourfold improvement arises from the presence of the cmnm(5) moiety. Measurements of Gln-tRNA(Gln) interactions at the ribosome A-site show that the s(2)U modification enhances binding affinity to the glutamine codons CAA and CAG and increases the rate of GTP hydrolysis by E. coli EF-Tu by fivefold.
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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.