ArticleNucleic acids research2020
eIF4G-driven translation initiation of downstream ORFs in mammalian cells.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Review
- Canonical translation factors eIF1A and eIF5B modulate the initiation step of repeat-associated non-AUG translation.Nucleic acids research · 2025Article
- Cell Reprogramming and Differentiation Utilizing Messenger RNA for Regenerative Medicine.Journal of developmental biology · 2023Review
- A viral pan-end RNA element and host complex define a SARS-CoV-2 regulon.Nature communications · 2023Article
- A widely applicable and cost-effective method for specific RNA-protein complex isolation.Scientific reports · 2023Article
- Three-nucleotide periodicity of nucleotide diversity in a population enables the identification of open reading frames.Briefings in bioinformatics · 2022Article
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Authors and funding
9 authors.
Funding
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Abstract
Comprehensive genome-wide analysis has revealed the presence of translational elements in the 3' untranslated regions (UTRs) of human transcripts. However, the mechanisms by which translation is initiated in 3' UTRs and the physiological function of their products remain unclear. This study showed that eIF4G drives the translation of various downstream open reading frames (dORFs) in 3' UTRs. The 3' UTR of GCH1, which encodes GTP cyclohydrolase 1, contains an internal ribosome entry site (IRES) that initiates the translation of dORFs. An in vitro reconstituted translation system showed that the IRES in the 3' UTR of GCH1 required eIF4G and conventional translation initiation factors, except eIF4E, for AUG-initiated translation of dORFs. The 3' UTR of GCH1-mediated translation was resistant to the mTOR inhibitor Torin 1, which inhibits cap-dependent initiation by increasing eIF4E-unbound eIF4G. eIF4G was also required for the activity of various elements, including polyU and poliovirus type 2, a short element thought to recruit ribosomes by base-pairing with 18S rRNA. These findings indicate that eIF4G mediates translation initiation of various ORFs in mammalian cells, suggesting that the 3' UTRs of mRNAs may encode various products.
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