ArticleNucleic acids research2015
Conformational changes in the P site and mRNA entry channel evoked by AUG recognition in yeast translation preinitiation complexes.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Structural Insights into the Mammalian Late-Stage Initiation Complexes.Cell reports · 2020Article
- Extensions, Extra Factors, and Extreme Complexity: Ribosomal Structures Provide Insights into Eukaryotic Translation.Cold Spring Harbor perspectives in biology · 2019Review
- The Jigsaw Puzzle of mRNA Translation Initiation in Eukaryotes: A Decade of Structures Unraveling the Mechanics of the Process.Annual review of biophysics · 2018Article
- Article
- ABCE1: A special factor that orchestrates translation at the crossroad between recycling and initiation.RNA biology · 2017Review
- 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
- Article
- Principles of start codon recognition in eukaryotic translation initiation.Nucleic acids research · 2016Article
- Review
- Sliding of a 43S ribosomal complex from the recognized AUG codon triggered by a delay in eIF2-bound GTP hydrolysis.Nucleic acids research · 2016Article
- Conformational Differences between Open and Closed States of the Eukaryotic Translation Initiation Complex.Molecular cell · 2015Article
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
The translation preinitiation complex (PIC) is thought to assume an open conformation when scanning the mRNA leader, with AUG recognition evoking a closed conformation and more stable P site interaction of Met-tRNAi; however, physical evidence is lacking that AUG recognition constrains interaction of mRNA with the 40S binding cleft. We compared patterns of hydroxyl radical cleavage of rRNA by Fe(II)-BABE tethered to unique sites in eIF1A in yeast PICs reconstituted with mRNA harboring an AUG or near-cognate (AUC) start codon. rRNA residues in the P site display reduced cleavage in AUG versus AUC PICs; and enhanced cleavage in the AUC complexes was diminished by mutations of scanning enhancer elements of eIF1A that increase near-cognate recognition in vivo. This suggests that accessibility of these rRNA residues is reduced by accommodation of Met-tRNAi in the P site (PIN state) and by their interactions with the anticodon stem of Met-tRNAi. Our cleavage data also provide evidence that AUG recognition evokes dissociation of eIF1 from its 40S binding site, ejection of the eIF1A-CTT from the P-site and rearrangement to a closed conformation of the entry channel with reduced mobility of mRNA.
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Registered trials
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.