Dataset Information

Yeast eIF4A enhances recruitment of mRNAs regardless of their structural complexity.

ABSTRACT: eIF4A is a DEAD-box RNA-dependent ATPase thought to unwind RNA secondary structure in the 5'-untranslated regions (UTRs) of mRNAs to promote their recruitment to the eukaryotic translation pre-initiation complex (PIC). We show that eIF4A's ATPase activity is markedly stimulated in the presence of the PIC, independently of eIF4E•eIF4G, but dependent on subunits i and g of the heteromeric eIF3 complex. Surprisingly, eIF4A accelerated the rate of recruitment of all mRNAs tested, regardless of their degree of structural complexity. Structures in the 5'-UTR and 3' of the start codon synergistically inhibit mRNA recruitment in a manner relieved by eIF4A, indicating that the factor does not act solely to melt hairpins in 5'-UTRs. Our findings that eIF4A functionally interacts with the PIC and plays important roles beyond unwinding 5'-UTR structure is consistent with a recent proposal that eIF4A modulates the conformation of the 40S ribosomal subunit to promote mRNA recruitment.

SUBMITTER: Yourik P

PROVIDER: S-EPMC5726853 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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Publications

Yeast eIF4A enhances recruitment of mRNAs regardless of their structural complexity.

Yourik Paul P Aitken Colin Echeverría CE Zhou Fujun F Gupta Neha N Hinnebusch Alan G AG Lorsch Jon R JR

eLife 20171130

eIF4A is a DEAD-box RNA-dependent ATPase thought to unwind RNA secondary structure in the 5'-untranslated regions (UTRs) of mRNAs to promote their recruitment to the eukaryotic translation pre-initiation complex (PIC). We show that eIF4A's ATPase activity is markedly stimulated in the presence of the PIC, independently of eIF4E•eIF4G, but dependent on subunits i and g of the heteromeric eIF3 complex. Surprisingly, eIF4A accelerated the rate of recruitment of all mRNAs tested, regardless of their ...[more]

PMID: 29192585

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Project description:The intricate relationship between multisensory integration and attention has been extensively researched in the multisensory field; however, the necessity of attention for the binding of multisensory stimuli remains contested. In the current study, we investigated whether diverting attention from well-known multisensory tasks would disrupt integration and whether the complexity of the stimulus and task modulated this interaction. A secondary objective of this study was to investigate individual differences in the interaction of attention and multisensory integration. Participants completed a simple audiovisual speeded detection task and McGurk task under various perceptual load conditions: no load (multisensory task while visual distractors present), low load (multisensory task while detecting the presence of a yellow letter in the visual distractors), and high load (multisensory task while detecting the presence of a number in the visual distractors). Consistent with prior studies, we found that increased perceptual load led to decreased reports of the McGurk illusion, thus confirming the necessity of attention for the integration of speech stimuli. Although increased perceptual load led to longer response times for all stimuli in the speeded detection task, participants responded faster on multisensory trials than unisensory trials. However, the increase in multisensory response times violated the race model for no and low perceptual load conditions only. Additionally, a geometric measure of Miller's inequality showed a decrease in multisensory integration for the speeded detection task with increasing perceptual load. Surprisingly, we found diverging changes in multisensory integration with increasing load for participants who did not show integration for the no load condition: no changes in integration for the McGurk task with increasing load but increases in integration for the detection task. The results of this study indicate that attention plays a crucial role in multisensory integration for both highly complex and simple multisensory tasks and that attention may interact differently with multisensory processing in individuals who do not strongly integrate multisensory information.

Dataset Information

Yeast eIF4A enhances recruitment of mRNAs regardless of their structural complexity.

Publications

Yeast eIF4A enhances recruitment of mRNAs regardless of their structural complexity.

Similar Datasets

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