ArticleeLife2019
An mRNA-binding channel in the ES6S region of the translation 48S-PIC promotes RNA unwinding and scanning.
Article in eLife, 2019. 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, 15 citations in OpenAlex.
- Streamlined synthetic regulatory cassette for efficient and photoreceptor-enriched retinal gene expression.Molecular therapy. Nucleic acids · 2026Article
- The differential effect of SARS-CoV-2 NSP1 on mRNA translation and stability reveals new insights linking ribosome recruitment, codon usage, and virus evolution.Nucleic acids research · 2025Article
- Progressive alterations in polysomal architecture and activation of ribosome stalling relief factors in a mouse model of Huntington's disease.Neurobiology of disease · 2024Article
- The molecular basis of translation initiation and its regulation in eukaryotes.Nature reviews. Molecular cell biology · 2024Review
- A widely applicable and cost-effective method for specific RNA-protein complex isolation.Scientific reports · 2023Article
- Ribosome heterogeneity and specialization of Plasmodium parasites.PLoS pathogens · 2023Article
- Action and function of helicases on RNA G-quadruplexes.Methods (San Diego, Calif.) · 2022Review
- Ribosome Biogenesis in Archaea.Frontiers in microbiology · 2021Review
- Mapping mRNA-18S rRNA Contacts Within Translation Initation Complexby Means of Reverse Transcriptase Termination Sites and RNAseq.Bio-protocol · 2020Article
- Translation-Associated Mutational U-Pressure in the First ORF of SARS-CoV-2 and Other Coronaviruses.Frontiers in microbiology · 2020Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Loading of mRNA onto the ribosomal 43S pre-initiation complex (PIC) and its subsequent scanning require the removal of the secondary structure of the by RNA helicases such as eIF4A. However, the topology and mechanics of the scanning complex bound to mRNA (48S-PIC) and the influence of its solvent-side composition on the scanning process are poorly known. Here, we found that the ES6S region of the 48S-PIC constitutes an extended binding channel for eIF4A-mediated unwinding of mRNA and scanning. Blocking ES6S inhibited the cap-dependent translation of mRNAs that have structured 5' UTRs (including G-quadruplexes), many of which are involved in signal transduction and growth, but it did not affect IRES-driven translation. Genome-wide analysis of mRNA translation revealed a great diversity in ES6S-mediated scanning dependency. Our data suggest that mRNA threading into the ES6S region makes scanning by 48S PIC slower but more processive. Hence, we propose a topological and functional model of the scanning 48S-PIC.
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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.