Cellular translational enhancer elements that recruit eukaryotic initiation factor 3.

Autor:	Koubek J; Yale University., Kaur J; Yale University., Bhandarkar S; Yale University., Lewis CJT; Yale University., Niederer RO; Yale University., Stanciu A; Vassar College., Aitken CE; Vassar College., Gilbert WV; Yale University; wendy.gilbert@yale.edu.
Jazyk:	angličtina
Zdroj:	RNA (New York, N.Y.) [RNA] 2024 Dec 04. Date of Electronic Publication: 2024 Dec 04.
DOI:	10.1261/rna.080310.124
Abstrakt:	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. (Published by Cold Spring Harbor Laboratory Press for the RNA Society.)
Databáze:	MEDLINE
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