New Structural Insights into Translational Miscoding.

Alexey Rozov, Natalia Demeshkina, Eric Westhof, Marat Yusupov, Gulnara Yusupova

Journal: Trends in biochemical sciences 2017;41(9):798-814

PMID: 27372401

Full Text on Elsevier Science View on PubMed

Abstract

The fidelity of translation depends strongly on the selection of the correct aminoacyl-tRNA that is complementary to the mRNA codon present in the ribosomal decoding center. The ribosome occasionally makes mistakes by selecting the wrong substrate from the pool of aminoacyl-tRNAs. Here, we summarize recent structural advances that may help to clarify the origin of missense errors that occur during decoding. These developments suggest that discrimination between tRNAs is based primarily on steric complementarity and shape acceptance rather than on the number of hydrogen bonds between the molding of the decoding center and the codon-anticodon duplex. They strengthen the hypothesis that spatial mimicry, due either to base tautomerism or ionization, drives infidelity in ribosomal translation.

Address: Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, CNRS, UMR7104/INSERM, U964/University of Strasbourg, Strasbourg, France.; Architecture and Reactivity of RNA, Institute of Molecular and Cellular Biology of the CNRS UPR9002/University of Strasbourg, Strasbourg, France.; Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, CNRS, UMR7104/INSERM, U964/University of Strasbourg, Strasbourg, France. Electronic address: [email protected].

DOI: 10.1016/j.tibs.2016.06.001

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MeSH Terms: Anticodon, Codon, Genetic Code, Hydrogen Bonding, Mutation, Missense, Protein Biosynthesis, RNA, Transfer, Amino Acid-Specific, Ribosomes