ArticleProceedings of the National Academy of Sciences of the United States of America1999
Correlation of deformability at a tRNA recognition site and aminoacylation specificity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
- Analysis of tRNA Aminoacylation by Northern Blotting and Multiplex Small RNA-Seq.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Benchmarking the Base Randomization Algorithm as a Possible Tool for the Initial Step of Generating a Virtual RNA Aptamers Library.Biotech (Basel (Switzerland)) · 2025Article
- High-resolution structure of stem-loop 4 from the 5'-UTR of SARS-CoV-2 solved by solution state NMR.Nucleic acids research · 2023Article
- Transfer RNAs: diversity in form and function.RNA biology · 2021Review
- Stereospecificity control in aminoacyl-tRNA-synthetases: new evidence of d-amino acids activation and editing.Nucleic acids research · 2019Article
- Article
- An innate twist between Crick's wobble and Watson-Crick base pairs.RNA (New York, N.Y.) · 2013Review
- Structure of the cytosine-cytosine mismatch in the thymidylate synthase mRNA binding site and analysis of its interaction with the aminoglycoside paromomycin.RNA (New York, N.Y.) · 2009Article
- Surprising contribution to aminoacylation and translation of non-Watson-Crick pairs in tRNA.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Structural and evolutionary classification of G/U wobble basepairs in the ribosome.Nucleic acids research · 2006Article
- Recognition of acceptor-stem structure of tRNA(Asp) by Escherichia coli aspartyl-tRNA synthetase.RNA (New York, N.Y.) · 2003Article
- The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism.The EMBO journal · 2001Article
- The G x U wobble base pair. A fundamental building block of RNA structure crucial to RNA function in diverse biological systems.EMBO reports · 2000Review
- On the wobble GoU and related pairs.RNA (New York, N.Y.) · 2000Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The fidelity of protein synthesis depends on specific tRNA aminoacylation by aminoacyl-tRNA synthetase enzymes, which in turn depends on the recognition of the identity of particular nucleotides and structural features in the substrate tRNA. These features generally reside within the acceptor helix, the anticodon stem-loop, and in some systems the variable pocket of the tRNA. In the alanine system, fidelity is ensured by a G.U wobble base pair located at the third position within the acceptor helix of alanine tRNA. We have investigated the activity of mutant alanine tRNAs to explore the mechanism of enzyme recognition. Here we show that the mismatched pair C-C is an excellent substitute for G.U in alanine-tRNA-knockout cells. A structural investigation by NMR spectroscopy of the C-C RNA acceptor end reveals that the two cytosines are intercalated into the helix, and that C-C exists in multiple conformations. Structural heterogeneity also is present in the wild-type G.U RNA, whereas inactive Watson-Crick helices are structurally rigid. The correlation between functional and structural data suggests that the G.U pair provides a distinctive structure and a point of deformability that allow the tRNA acceptor end to fit into the active site of the alanyl-tRNA synthetase. Fidelity is ensured because noncognate and inactive mutant tRNAs are bound in the active site in an incorrect conformation that reduces enzymatic activity.
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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.