ArticleGenes & development2014
Conserved residues in yeast initiator tRNA calibrate initiation accuracy by regulating preinitiation complex stability at the start codon.
Article in Genes & development, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- Distinct uS11/Rps14 interactions with the translation preinitiation complex differentially alter the accuracy of start codon recognition.Nucleic acids research · 2025Article
- eIF2α interactions with mRNA control accurate start codon selection by the translation preinitiation complex.Nucleic acids research · 2020Article
- Structural basis for the transition from translation initiation to elongation by an 80S-eIF5B complex.Nature communications · 2020Article
- A network of eIF2β interactions with eIF1 and Met-tRNAi promotes accurate start codon selection by the translation preinitiation complex.Nucleic acids research · 2019Article
- MEHMO syndrome mutation EIF2S3-I259M impairs initiator Met-tRNAiMet binding to eukaryotic translation initiation factor eIF2.Nucleic acids research · 2019Article
- Protein Synthesis Initiation in Eukaryotic Cells.Cold Spring Harbor perspectives in biology · 2018Review
- eIF1 Loop 2 interactions with Met-tRNAProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Rps3/uS3 promotes mRNA binding at the 40S ribosome entry channel and stabilizes preinitiation complexes at start codons.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Two highly conserved features of bacterial initiator tRNAs license them to pass through distinct checkpoints in translation initiation.Nucleic acids research · 2017Article
- Structure of a 30S pre-initiation complex stalled by GE81112 reveals structural parallels in bacterial and eukaryotic protein synthesis initiation pathways.Nucleic acids research · 2017Article
- Review
- Ribosome Structure Reveals Preservation of Active Sites in the Presence of a P-Site Wobble Mismatch.Structure (London, England : 1993) · 2015Article
- Conformational Differences between Open and Closed States of the Eukaryotic Translation Initiation Complex.Molecular cell · 2015Article
- Article
- Conformational changes in the P site and mRNA entry channel evoked by AUG recognition in yeast translation preinitiation complexes.Nucleic acids research · 2015Article
- Is the cellular initiation of translation an exclusive property of the initiator tRNAs?RNA biology · 2015Article
- Human eukaryotic initiation factor 2 (eIF2)-GTP-Met-tRNAi ternary complex and eIF3 stabilize the 43 S preinitiation complex.The Journal of biological chemistry · 2014Article
- Structural changes enable start codon recognition by the eukaryotic translation initiation complex.Cell · 2014Article
- An extended Shine-Dalgarno sequence in mRNA functionally bypasses a vital defect in initiator tRNA.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Eukaryotic initiator tRNA (tRNAi) contains several highly conserved unique sequence features, but their importance in accurate start codon selection was unknown. Here we show that conserved bases throughout tRNAi, from the anticodon stem to acceptor stem, play key roles in ensuring the fidelity of start codon recognition in yeast cells. Substituting the conserved G31:C39 base pair in the anticodon stem with different pairs reduces accuracy (the Sui(-) [suppressor of initiation codon] phenotype), whereas eliminating base pairing increases accuracy (the Ssu(-) [suppressor of Sui(-)] phenotype). The latter defect is fully suppressed by a Sui(-) substitution of T-loop residue A54. These genetic data are paralleled by opposing effects of Sui(-) and Ssu(-) substitutions on the stability of methionylated tRNAi (Met-tRNA(i)) binding (in the ternary complex [TC] with eIF2-GTP) to reconstituted preinitiation complexes (PICs). Disrupting the C3:G70 base pair in the acceptor stem produces a Sui(-) phenotype and also reduces the rate of TC binding to 40S subunits in vitro and in vivo. Both defects are suppressed by an Ssu(-) substitution in eIF1A that stabilizes the open/P(OUT) conformation of the PIC that exists prior to start codon recognition. Our data indicate that these signature sequences of tRNA(i) regulate accuracy by distinct mechanisms, promoting the open/P(OUT) conformation of the PIC (for C3:G70) or destabilizing the closed/P(IN) state (for G31:C39 and A54) that is critical for start codon recognition.
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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.