Abstract
During transfer RNA (tRNA) selection, a cognate codon:anticodon interaction triggers a series of events that ultimately results in the acceptance of that tRNA into the ribosome for peptide-bond formation. High-fidelity discrimination between the cognate tRNA and near- and noncognate ones depends both on their differential dissociation rates from the ribosome and on specific acceleration of forward rate constants by cognate species. Here we show that a mutant tRNA(Trp) carrying a single substitution in its D-arm achieves elevated levels of miscoding by accelerating these forward rate constants independent of codon:anticodon pairing in the decoding center. These data provide evidence for a direct role for tRNA in signaling its own acceptance during decoding and support its fundamental role during the evolution of protein synthesis.
MeSH Terms
Anticodon
Base Pairing
Codon
Codon, Terminator
Dipeptides/biosynthesis
GTP Phosphohydrolases/metabolism
Guanosine Triphosphate/metabolism
Hydrolysis
Kinetics
Mutation
Nucleic Acid Conformation
Peptide Elongation Factor Tu/metabolism
Protein Biosynthesis
RNA, Messenger/metabolism
RNA, Transfer, Trp/chemistry,genetics,metabolism
Ribosomes/metabolism
Chemicals
Anticodon
Codon
Codon, Terminator
Dipeptides
RNA, Messenger
RNA, Transfer, Trp
Guanosine Triphosphate
GTP Phosphohydrolases
Peptide Elongation Factor Tu
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Cochella Luisa
Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Green Rachel
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