ArticleJournal of molecular biology2012
Human tRNA(Lys3)(UUU) is pre-structured by natural modifications for cognate and wobble codon binding through keto-enol tautomerism.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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79 citing papers in PubMed, 122 citations in OpenAlex.
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- Elp3 uses a conserved molecular tunnel to transport acetate between distant active sites and catalyze tRNA wobble base modification.Nature communications · 2026Article
- Recognition of the wobble pair: quantum mechanical calculations of tRNA U34 or C34 modifications within the ribosomal decoding center.Nucleic acids research · 2026Article
- Translational regulation by oxidative desulfuration of tRNA modifications.Nature communications · 2026Article
- Uridines Modified with Sulfur or Selenium in U-G Wobble Pairs Matter for tRNA Function.Current medicinal chemistry · 2026Review
- Transfer RNA Aspartic Acid Methyltransferase 1 (TRDMT1/DNMT2) Regulates Plant Development and Gene Expression in the Moss Physcomitrium patens.Molecular genetics and genomics : MGG · 2025Article
- Structural Impact of 3-methylcytosine Modification on the Anticodon Stem-loop of a Neuronally-enriched Arginine tRNA.Journal of molecular biology · 2025Article
- Loss of both wobbleUFrontiers in plant science · 2025Article
- Structural insights into the decoding capability of isoleucine tRNAs with lysidine and agmatidine.Nature structural & molecular biology · 2024Article
- NMR measurements of transient low-populated tautomeric and anionic Watson-Crick-like G·T/U in RNA:DNA hybrids: implications for the fidelity of transcription and CRISPR/Cas9 gene editing.Nucleic acids research · 2024Article
- Anticodon stem-loop tRNA modifications influence codon decoding and frame maintenance during translation.Seminars in cell & developmental biology · 2024Review
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Streptothricin F is a bactericidal antibiotic effective against highly drug-resistant gram-negative bacteria that interacts with the 30S subunit of the 70S ribosome.PLoS biology · 2023Article
- Cryo-EM structure of the fully assembled Elongator complex.Nucleic acids research · 2023Article
- Epitranscriptome: Review of Top 25 Most-Studied RNA Modifications.International journal of molecular sciences · 2022Review
- 2-Selenouridine, a Modified Nucleoside of Bacterial tRNAs, Its Reactivity in the Presence of Oxidizing and Reducing Reagents.International journal of molecular sciences · 2022Article
- Review
- Biochemical and Structural Characterization of Human Core Elongator and Its Subassemblies.ACS omega · 2022Article
- Crystal structure of human METTL6, the mCommunications biology · 2021Article
19 more citing papers are in PubMed but not listed here.
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8 authors at 4 institutions in 2 countries.
Funding
Abstract
Human tRNA(Lys3)(UUU) (htRNA(Lys3)(UUU)) decodes the lysine codons AAA and AAG during translation and also plays a crucial role as the primer for HIV-1 (human immunodeficiency virus type 1) reverse transcription. The posttranscriptional modifications 5-methoxycarbonylmethyl-2-thiouridine (mcm(5)s(2)U(34)), 2-methylthio-N(6)-threonylcarbamoyladenosine (ms(2)t(6)A(37)), and pseudouridine (Ψ(39)) in the tRNA's anticodon domain are critical for ribosomal binding and HIV-1 reverse transcription. To understand the importance of modified nucleoside contributions, we determined the structure and function of this tRNA's anticodon stem and loop (ASL) domain with these modifications at positions 34, 37, and 39, respectively (hASL(Lys3)(UUU)-mcm(5)s(2)U(34);ms(2)t(6)A(37);Ψ(39)). Ribosome binding assays in vitro revealed that the hASL(Lys3)(UUU)-mcm(5)s(2)U(34);ms(2)t(6)A(37);Ψ(39) bound AAA and AAG codons, whereas binding of the unmodified ASL(Lys3)(UUU) was barely detectable. The UV hyperchromicity, the circular dichroism, and the structural analyses indicated that Ψ(39) enhanced the thermodynamic stability of the ASL through base stacking while ms(2)t(6)A(37) restrained the anticodon to adopt an open loop conformation that is required for ribosomal binding. The NMR-restrained molecular-dynamics-derived solution structure revealed that the modifications provided an open, ordered loop for codon binding. The crystal structures of the hASL(Lys3)(UUU)-mcm(5)s(2)U(34);ms(2)t(6)A(37);Ψ(39) bound to the 30S ribosomal subunit with each codon in the A site showed that the modified nucleotides mcm(5)s(2)U(34) and ms(2)t(6)A(37) participate in the stability of the anticodon-codon interaction. Importantly, the mcm(5)s(2)U(34)·G(3) wobble base pair is in the Watson-Crick geometry, requiring unusual hydrogen bonding to G in which mcm(5)s(2)U(34) must shift from the keto to the enol form. The results unambiguously demonstrate that modifications pre-structure the anticodon as a key prerequisite for efficient and accurate recognition of cognate and wobble codons.
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