ArticleNucleic acids research1997
Structural studies on tRNA acceptor stem microhelices: exchange of the discriminator base A73 for G in human tRNALeu switches the acceptor specificity from leucine to serine possibly by decreasing the stability of the terminal G1-C72 base pair.
Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- tRNA Metabolism and Neurodevelopmental Disorders.Annual review of genomics and human genetics · 2019Review
- LeuRS can leucylate type I and type II tRNALeus in Streptomyces coelicolor.Nucleic acids research · 2019Article
- Molecular reconstruction of a fungal genetic code alteration.RNA biology · 2013Article
- Recognition of tRNALeu by Aquifex aeolicus leucyl-tRNA synthetase during the aminoacylation and editing steps.Nucleic acids research · 2008Article
- Effect of G-1 on histidine tRNA microhelix conformation.Nucleic acids research · 2003Article
- Identification of essential domains for Escherichia coli tRNA(leu) aminoacylation and amino acid editing using minimalist RNA molecules.Nucleic acids research · 2002Article
- Importance of discriminator base stacking interactions: molecular dynamics analysis of A73 microhelix(Ala) variants.Nucleic acids research · 2000Article
- Activation of microhelix charging by localized helix destabilization.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
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7 authors at 1 institution in 1 country.
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Abstract
Correct recognition of transfer RNAs (tRNAs) by aminoacyl-tRNA synthetases (aaRS) is crucial to the maintenance of translational fidelity. The discriminator base A73 in human tRNALeuis critical for its specific recognition by the aaRS. Exchanging A73 for G abolishes leucine acceptance and converts it into a serine acceptor in vitro . Two RNA microhelices of 24 nt length that correspond to the tRNALeuacceptor stem and differ only in the discriminator base were synthesized: a wild-type tRNALeumicrohelix, where nt 21 corresponds to the discriminator base position 73, and an A21G mutant microhelix. To investigate whether different identities of both tRNAs are caused by conformational differences, NMR and UV melting experiments were performed on both microhelices. Two-dimentional NOESY spectra showed both microhelices to exhibit the same overall conformation at their 3'-CCA ends. Thermodynamic analysis and melting behaviour of the base-paired imino protons observed by NMR spectroscopy suggest that the A21G (A73G in tRNA) exchange results in a decrease of melting transition cooperativity and a destabilization of the terminal G1-C20 (G1-C72 in tRNA) base pair. Furthermore, the fact that this 3'-terminal imino proton is more solvent-exposed at physiological temperature might be another indication for the importance of the stability of the terminal base pair for specific tRNA recognition.
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