ArticleProceedings of the National Academy of Sciences of the United States of America2006
Surprising contribution to aminoacylation and translation of non-Watson-Crick pairs in tRNA.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
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- Article
- On the role of Hoogsteen:Hoogsteen interactions in RNA: ab initio investigations of structures and energies.RNA (New York, N.Y.) · 2010Article
- Analysis of genomic tRNA sets from Bacteria, Archaea, and Eukarya points to anticodon-codon hydrogen bonds as a major determinant of tRNA compositional variations.RNA (New York, N.Y.) · 2008Article
- Pyrrolysine is not hardwired for cotranslational insertion at UAG codons.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Structural elements defining elongation factor Tu mediated suppression of codon ambiguity.Nucleic acids research · 2007Article
- Diversity of tRNA genes in eukaryotes.Nucleic acids research · 2006Article
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1 author.
Funding
Abstract
Molecules of transfer RNA (tRNA) typically contain four stems composed of Watson-Crick (W-C) base pairs and infrequent mispairs such as G-U and A-C. The latter mispairs are fundamental units of RNA secondary structure found in nearly every class of RNA and are nearly isomorphic to W-C pairs. Therefore, they often substitute for G-C or A-U base pairs. The mispairs also have unique chemical, structural, and dynamic conformational properties, which can only be partially mimicked by W-C base pairs. Here, I characterize the identities and tasks of six mutant G-U and A-C mispairs in Escherichia coli tRNA(Gly) using genetic and bioinformatic tools and show that mispairs are significantly more important for aminoacylation and translation than previously realized. Mispairs boost aminoacylation and translation primarily because they activate tRNA by means of their conformational flexibility. The statistical preservation of the six mutant mispair sites across tRNA(Gly) in many organisms points to a fundamental structure-function signature within tRNA(Gly) with possible analogous missions in other RNAs.
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