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Elife. 2016 Aug 5;5. pii: e16408. doi: 10.7554/eLife.16408.

Coupling between the DEAD-box RNA helicases Ded1p and eIF4A.

Author information

1
Center for RNA Molecular Biology, Case Western Reserve University, Cleveland, United States.
2
Department of Biochemistry, Case Western Reserve University, Cleveland, United States.
3
School of Medicine, Case Western Reserve University, Cleveland, United States.
4
Department of Biology, University of Richmond, Richmond, United States.

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.

KEYWORDS:

RNA; S. cerevisiae; biochemistry; helicase; none; translation

PMID:
27494274
PMCID:
PMC4990422
DOI:
10.7554/eLife.16408
[Indexed for MEDLINE]
Free PMC Article

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