Coupling between the DEAD-box RNA helicases Ded1p and eIF4A.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 27494274.
- Also identified by DOI 10.7554/eLife.16408 and PMC identifier 4990422.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Eukaryotic translation initiation involves two conserved DEAD-box RNA helicases, eIF4A and Ded1p. Here we show that S. cerevisiae eIF4A and Ded1p directly interact with each other and simultaneously with the scaffolding protein eIF4G. We delineate a comprehensive thermodynamic framework for the interactions between Ded1p, eIF4A, eIF4G, RNA and ATP, which indicates that eIF4A, with and without eIF4G, acts as a modulator for activity and substrate preferences of Ded1p, which is the RNA remodeling unit in all complexes. Our results reveal and characterize an unexpected interdependence between the two RNA helicases and eIF4G, and suggest that Ded1p is an integral part of eIF4F, the complex comprising eIF4G, eIF4A, and eIF4E.
Medical subject headings
- DEAD-box RNA Helicases
- Eukaryotic Initiation Factor-4A
- Eukaryotic Initiation Factor-4G
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins