Coupling between the DEAD-box RNA helicases Ded1p and eIF4A

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 inte...

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Autores principales: Gao, Zhaofeng, Putnam, Andrea A, Bowers, Heath A, Guenther, Ulf-Peter, Ye, Xuan, Kindsfather, Audrey, Hilliker, Angela K, Jankowsky, Eckhard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2016
Materias:
Biochemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4990422/
https://www.ncbi.nlm.nih.gov/pubmed/27494274
http://dx.doi.org/10.7554/eLife.16408
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author Gao, Zhaofeng
Putnam, Andrea A
Bowers, Heath A
Guenther, Ulf-Peter
Ye, Xuan
Kindsfather, Audrey
Hilliker, Angela K
Jankowsky, Eckhard
author_facet Gao, Zhaofeng
Putnam, Andrea A
Bowers, Heath A
Guenther, Ulf-Peter
Ye, Xuan
Kindsfather, Audrey
Hilliker, Angela K
Jankowsky, Eckhard
author_sort Gao, Zhaofeng
collection PubMed
description 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. DOI: http://dx.doi.org/10.7554/eLife.16408.001
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spelling pubmed-49904222016-08-19 Coupling between the DEAD-box RNA helicases Ded1p and eIF4A Gao, Zhaofeng Putnam, Andrea A Bowers, Heath A Guenther, Ulf-Peter Ye, Xuan Kindsfather, Audrey Hilliker, Angela K Jankowsky, Eckhard eLife Biochemistry 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. DOI: http://dx.doi.org/10.7554/eLife.16408.001 eLife Sciences Publications, Ltd 2016-08-05 /pmc/articles/PMC4990422/ /pubmed/27494274 http://dx.doi.org/10.7554/eLife.16408 Text en © 2016, Gao et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Biochemistry
Gao, Zhaofeng
Putnam, Andrea A
Bowers, Heath A
Guenther, Ulf-Peter
Ye, Xuan
Kindsfather, Audrey
Hilliker, Angela K
Jankowsky, Eckhard
Coupling between the DEAD-box RNA helicases Ded1p and eIF4A
title Coupling between the DEAD-box RNA helicases Ded1p and eIF4A
title_full Coupling between the DEAD-box RNA helicases Ded1p and eIF4A
title_fullStr Coupling between the DEAD-box RNA helicases Ded1p and eIF4A
title_full_unstemmed Coupling between the DEAD-box RNA helicases Ded1p and eIF4A
title_short Coupling between the DEAD-box RNA helicases Ded1p and eIF4A
title_sort coupling between the dead-box rna helicases ded1p and eif4a
topic Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4990422/
https://www.ncbi.nlm.nih.gov/pubmed/27494274
http://dx.doi.org/10.7554/eLife.16408
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