ArticleNucleic acids research2019
A network of eIF2β interactions with eIF1 and Met-tRNAi promotes accurate start codon selection by the translation preinitiation complex.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Site-specific inhibition of translation initiation via 2'-O-methylation.Nucleic acids research · 2026Article
- Distinct uS11/Rps14 interactions with the translation preinitiation complex differentially alter the accuracy of start codon recognition.Nucleic acids research · 2025Article
- Functional screen identifies RBM42 as a mediator of oncogenic mRNA translation specificity.Nature cell biology · 2025Article
- Structural basis for translational control by the human 48S initiation complex.Nature structural & molecular biology · 2025Article
- Structural basis of AUC codon discrimination during translation initiation in yeast.Nucleic acids research · 2024Article
- eIF2β zinc-binding domain interacts with the eIF2γ subunit through the guanine nucleotide binding interface to promote Met-tRNAiMet binding.Bioscience reports · 2024Article
- Inhibitors of eIF4G1-eIF1 uncover its regulatory role of ER/UPR stress-response genes independent of eIF2α-phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Selection of start codon during mRNA scanning in eukaryotic translation initiation.Communications biology · 2022Article
- Structural Differences in Translation Initiation between Pathogenic Trypanosomatids and Their Mammalian Hosts.Cell reports · 2020Article
- eIF2α interactions with mRNA control accurate start codon selection by the translation preinitiation complex.Nucleic acids research · 2020Article
- 5'-UTR recruitment of the translation initiation factor eIF4GI or DAP5 drives cap-independent translation of a subset of human mRNAs.The Journal of biological chemistry · 2020Article
- Non-AUG start codons: Expanding and regulating the small and alternative ORFeome.Experimental cell research · 2020Review
- eIF1 discriminates against suboptimal initiation sites to prevent excessive uORF translation genome-wide.RNA (New York, N.Y.) · 2020Article
- Control of Translation at the Initiation Phase During Glucose Starvation in Yeast.International journal of molecular sciences · 2019Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In translation initiation, a 43S preinitiation complex (PIC) containing eIF1 and a ternary complex (TC) of GTP-bound eIF2 and Met-RNAi scans the mRNA for the start codon. AUG recognition triggers eIF1 release and rearrangement from an open PIC conformation to a closed state with more tightly-bound Met-tRNAi (PIN state). Cryo-EM models reveal eIF2β contacts with eIF1 and Met-tRNAi exclusive to the open complex that should destabilize the closed state. eIF2β or eIF1 substitutions disrupting these contacts increase initiation at UUG codons, and compound substitutions also derepress translation of GCN4, indicating slower TC recruitment. The latter substitutions slow TC loading while stabilizing TC binding at UUG codons in reconstituted PICs, indicating a destabilized open complex and shift to the closed/PIN state. An eIF1 substitution that should strengthen the eIF2β:eIF1 interface has the opposite genetic and biochemical phenotypes. eIF2β is also predicted to restrict Met-tRNAi movement into the closed/PIN state, and substitutions that should diminish this clash increase UUG initiation in vivo and stabilize Met-tRNAi binding at UUG codons in vitro with little effect on TC loading. Thus, eIF2β anchors eIF1 and TC to the open complex, enhancing PIC assembly and scanning, while impeding rearrangement to the closed conformation at non-AUG codons.
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