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• W2155441706 abstract "In the current model of translation initiation by the scanning mechanism, eIF1 promotes an open conformation of the 40S subunit competent for rapidly loading the eIF2·GTP·Met-tRNA i ternary complex (TC) in a metastable conformation (P OUT ) capable of sampling triplets entering the P site while blocking accommodation of Met-tRNA i in the P IN state and preventing completion of GTP hydrolysis (P i release) by the TC. All of these functions should be reversed by eIF1 dissociation from the preinitiation complex (PIC) on AUG recognition. We tested this model by selecting eIF1 Ssu − mutations that suppress the elevated UUG initiation and reduced rate of TC loading in vivo conferred by an eIF1 (Sui − ) substitution that eliminates a direct contact of eIF1 with the 40S subunit. Importantly, several Ssu − substitutions increase eIF1 affinity for 40S subunits in vitro, and the strongest-binding variant (D61G), predicted to eliminate ionic repulsion with 18S rRNA, both reduces the rate of eIF1 dissociation and destabilizes the P IN state of TC binding in reconstituted PICs harboring Sui − variants of eIF5 or eIF2. These findings establish that eIF1 dissociation from the 40S subunit is required for the P IN mode of TC binding and AUG recognition and that increasing eIF1 affinity for the 40S subunit increases initiation accuracy in vivo. Our results further demonstrate that the GTPase-activating protein eIF5 and β-subunit of eIF2 promote accuracy by controlling eIF1 dissociation and the stability of TC binding to the PIC, beyond their roles in regulating GTP hydrolysis by eIF2." @default.
• W2155441706 created "2016-06-24" @default.
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• W2155441706 date "2013-12-13" @default.
• W2155441706 modified "2023-10-10" @default.
• W2155441706 title "Enhanced eIF1 binding to the 40S ribosome impedes conformational rearrangements of the preinitiation complex and elevates initiation accuracy" @default.
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• W2155441706 doi "https://doi.org/10.1261/rna.042069.113" @default.
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