ArticleNucleic acids research2022
Conformational rearrangements upon start codon recognition in human 48S translation initiation complex.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 42 citations in OpenAlex.
- Site-specific inhibition of translation initiation via 2'-O-methylation.Nucleic acids research · 2026Article
- Review
- Translation initiation by the Kozak mRNA sequence is based on a conformational readout on the ribosome.Nature communications · 2026Article
- Article
- A ribosomal kinetic checkpoint governs selective mRNA recruitment.bioRxiv : the preprint server for biology · 2026Article
- Toward a unifying mechanistic model of eukaryotic translation initiation through integrative single-molecule, structural, and computational insights.Current opinion in structural biology · 2026Review
- Translational control of Toxoplasma gondii differentiation.Bioscience reports · 2026Review
- Article
- Structural basis for non-AUG translation regulation by 5MPs.bioRxiv : the preprint server for biology · 2025Article
- eIF3: a critical player in mRNA recruitment to the ribosome with emerging roles across translation.Biochemical Society transactions · 2025Review
- Eukaryotic translation initiation factor 4F: functional properties and physiological role.Nucleic acids research · 2025Review
- Exploring the interaction dynamics of eukaryotic translation initiation factor 2.Biochemical Society transactions · 2025Review
- Distinct non-canonical translation initiation modes arise for specific host and viral mRNAs during poxvirus-induced shutoff.Nature microbiology · 2025Article
- Distinct uS11/Rps14 interactions with the translation preinitiation complex differentially alter the accuracy of start codon recognition.Nucleic acids research · 2025Article
- Ribosome customization and functional diversification among P-stalk proteins regulate late poxvirus protein synthesis.Cell reports · 2025Article
- Novel archaeal ribosome dimerization factor facilitating unique 30S-30S dimerization.Nucleic acids research · 2025Article
- Structural basis for translational control by the human 48S initiation complex.Nature structural & molecular biology · 2025Article
- LARP1 binds ribosomes and TOP mRNAs in repressed complexes.The EMBO journal · 2024Article
- Structural basis of LRPPRC-SLIRP-dependent translation by the mitoribosome.Nature structural & molecular biology · 2024Article
- Structural basis of AUC codon discrimination during translation initiation in yeast.Nucleic acids research · 2024Article
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Authors and funding
11 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Selection of the translation start codon is a key step during protein synthesis in human cells. We obtained cryo-EM structures of human 48S initiation complexes and characterized the intermediates of codon recognition by kinetic methods using eIF1A as a reporter. Both approaches capture two distinct ribosome populations formed on an mRNA with a cognate AUG codon in the presence of eIF1, eIF1A, eIF2-GTP-Met-tRNAiMet and eIF3. The 'open' 40S subunit conformation differs from the human 48S scanning complex and represents an intermediate preceding the codon recognition step. The 'closed' form is similar to reported structures of complexes from yeast and mammals formed upon codon recognition, except for the orientation of eIF1A, which is unique in our structure. Kinetic experiments show how various initiation factors mediate the population distribution of open and closed conformations until 60S subunit docking. Our results provide insights into the timing and structure of human translation initiation intermediates and suggest the differences in the mechanisms of start codon selection between mammals and yeast.
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