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dc.contributor.authorLuna, Rafael E.eng
dc.contributor.authorArthanari, Haribabueng
dc.contributor.authorHiraishi, Hiroyukieng
dc.contributor.authorNanda, Jagpreedeng
dc.contributor.authorMartin-Marcos, Pilareng
dc.contributor.authorMarkus, Michelle A.eng
dc.contributor.authorAkabayov, Barakeng
dc.contributor.authorMilbradt, Alexander G.eng
dc.contributor.authorLuna, Lunet E.eng
dc.contributor.authorSeo, Hee-Chaneng
dc.contributor.authorHyberts, Sven G.eng
dc.contributor.authorFahmy, Amreng
dc.contributor.authorReibarkh, Mikhaileng
dc.contributor.authorMiles, Davideng
dc.contributor.authorHagner, Patrick R.eng
dc.contributor.authorO'Day, Elizabeth M.eng
dc.contributor.authorYi, Tingfangeng
dc.contributor.authorMarintchev, Asseneng
dc.contributor.authorHinnebusch, Alan G.eng
dc.contributor.authorLorsch, John R.eng
dc.contributor.authorAsano, Katsuraeng
dc.contributor.authorWagner, Gerhardeng
dc.description.abstractRecognition of the proper start codon on mRNAs is essential for protein synthesis, which requires scanning and involves eukaryotic initiation factors (eIFs) eIF1, eIF1A, eIF2, and eIF5. The carboxyl terminal domain (CTD) of eIF5 stimulates 43S preinitiation complex (PIC) assembly; however, its precise role in scanning and start codon selection has remained unknown. Using nuclear magnetic resonance (NMR) spectroscopy, we identified the binding sites of eIF1 and eIF2β on eIF5-CTD and found that they partially overlapped. Mutating select eIF5 residues in the common interface specifically disrupts interaction with both factors. Genetic and biochemical evidence indicates that these eIF5-CTD mutations impair start codon recognition and impede eIF1 release from the PIC by abrogating eIF5-CTD binding to eIF2β. This study provides mechanistic insight into the role of eIF5-CTD's dynamic interplay with eIF1 and eIF2β in switching PICs from an open to a closed state at start codons.en_US
dc.rightsAttribution-NonCommercial-NoDerivs CC BY-NC-NDeng
dc.titleThe C-terminal domain of eukaryotic initiation factor 5 promotes start codon recognition by its dynamic interplay with eIF1 and eIF2 betaen_US
dc.typePeer reviewed
dc.typeJournal article
dc.rights.holderCopyright 2012 The Authorsen_US
dc.source.journalCell reports

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Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs CC BY-NC-ND