AI Article Synopsis
- Translation initiation significantly influences gene expression in eukaryotes, with eukaryotic initiation factor 3 (eIF3) playing a key role in recruiting ribosomes.
- This study examined how eIF3's binding to specific 5'-untranslated regions (5'-UTRs) of mRNAs leads to varying protein outputs, finding that it binds to a specific motif, AMAYAA, in some 5'-UTRs.
- The study demonstrates that mRNAs bound by eIF3 have higher ribosome density and are preferentially translated during stress, highlighting eIF3's role as a novel translational enhancer.
Article Abstract
Translation initiation is a highly regulated process which broadly affects eukaryotic gene expression. Eukaryotic initiation factor 3 (eIF3) is a central player in canonical and alternative pathways for ribosome recruitment. Here we have investigated how direct binding of eIF3 contributes to the large and regulated differences in protein output conferred by different 5'-untranslated regions (5'-UTRs) of cellular mRNAs. Using an unbiased high-throughput approach to determine the affinity of budding yeast eIF3 for native 5'-UTRs from 4,252 genes, we demonstrate that eIF3 binds specifically to a subset of 5'-UTRs that contain a short unstructured binding motif, AMAYAA. eIF3 binding mRNAs have higher ribosome density in growing cells and are preferentially translated under certain stress conditions, supporting the functional relevance of this interaction. Our results reveal a new class of translational enhancer and suggest a mechanism by which changes in core initiation factor activity enact mRNA-specific translation.
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| http://dx.doi.org/10.1261/rna.080310.124 | DOI Listing |
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