Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo

Yeast DEAD-box helicase Ded1 stimulates translation initiation, particularly of mRNAs with structured 5'UTRs. Interactions of the Ded1 N-terminal domain (NTD) with eIF4A, and Ded1-CTD with eIF4G, subunits of eIF4F, enhance Ded1 unwinding activity and stimulation of preinitiation complex (PIC) a...
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Autor*in:	Suna Gulay [verfasserIn] Neha Gupta [verfasserIn] Jon R Lorsch [verfasserIn] Alan G Hinnebusch [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	Ded1/Ddx3 RNA helicase eIF4E eIF4A eIF4G translation initiation

Übergeordnetes Werk:	In: eLife - eLife Sciences Publications Ltd, 2013, 9(2020)
Übergeordnetes Werk:	volume:9 ; year:2020

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.7554/eLife.58243

Katalog-ID:	DOAJ022140395

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520			\|a Yeast DEAD-box helicase Ded1 stimulates translation initiation, particularly of mRNAs with structured 5'UTRs. Interactions of the Ded1 N-terminal domain (NTD) with eIF4A, and Ded1-CTD with eIF4G, subunits of eIF4F, enhance Ded1 unwinding activity and stimulation of preinitiation complex (PIC) assembly in vitro. However, the importance of these interactions, and of Ded1-eIF4E association, in vivo were poorly understood. We identified separate amino acid clusters in the Ded1-NTD required for binding to eIF4A or eIF4E in vitro. Disrupting each cluster selectively impairs native Ded1 association with eIF4A or eIF4E, and reduces cell growth, polysome assembly, and translation of reporter mRNAs with structured 5'UTRs. It also impairs Ded1 stimulation of PIC assembly on a structured mRNA in vitro. Ablating Ded1 interactions with eIF4A/eIF4E unveiled a requirement for the Ded1-CTD for robust initiation. Thus, Ded1 function in vivo is stimulated by independent interactions of its NTD with eIF4E and eIF4A, and its CTD with eIF4G.
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allfields	10.7554/eLife.58243 doi (DE-627)DOAJ022140395 (DE-599)DOAJ75675e0e4795445bbe9ffffe87494d14 DE-627 ger DE-627 rakwb eng QH301-705.5 Suna Gulay verfasserin aut Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Yeast DEAD-box helicase Ded1 stimulates translation initiation, particularly of mRNAs with structured 5'UTRs. Interactions of the Ded1 N-terminal domain (NTD) with eIF4A, and Ded1-CTD with eIF4G, subunits of eIF4F, enhance Ded1 unwinding activity and stimulation of preinitiation complex (PIC) assembly in vitro. However, the importance of these interactions, and of Ded1-eIF4E association, in vivo were poorly understood. We identified separate amino acid clusters in the Ded1-NTD required for binding to eIF4A or eIF4E in vitro. Disrupting each cluster selectively impairs native Ded1 association with eIF4A or eIF4E, and reduces cell growth, polysome assembly, and translation of reporter mRNAs with structured 5'UTRs. It also impairs Ded1 stimulation of PIC assembly on a structured mRNA in vitro. Ablating Ded1 interactions with eIF4A/eIF4E unveiled a requirement for the Ded1-CTD for robust initiation. Thus, Ded1 function in vivo is stimulated by independent interactions of its NTD with eIF4E and eIF4A, and its CTD with eIF4G. Ded1/Ddx3 RNA helicase eIF4E eIF4A eIF4G translation initiation Medicine R Science Q Biology (General) Neha Gupta verfasserin aut Jon R Lorsch verfasserin aut Alan G Hinnebusch verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.58243 kostenfrei https://doaj.org/article/75675e0e4795445bbe9ffffe87494d14 kostenfrei https://elifesciences.org/articles/58243 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
spelling	10.7554/eLife.58243 doi (DE-627)DOAJ022140395 (DE-599)DOAJ75675e0e4795445bbe9ffffe87494d14 DE-627 ger DE-627 rakwb eng QH301-705.5 Suna Gulay verfasserin aut Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Yeast DEAD-box helicase Ded1 stimulates translation initiation, particularly of mRNAs with structured 5'UTRs. Interactions of the Ded1 N-terminal domain (NTD) with eIF4A, and Ded1-CTD with eIF4G, subunits of eIF4F, enhance Ded1 unwinding activity and stimulation of preinitiation complex (PIC) assembly in vitro. However, the importance of these interactions, and of Ded1-eIF4E association, in vivo were poorly understood. We identified separate amino acid clusters in the Ded1-NTD required for binding to eIF4A or eIF4E in vitro. Disrupting each cluster selectively impairs native Ded1 association with eIF4A or eIF4E, and reduces cell growth, polysome assembly, and translation of reporter mRNAs with structured 5'UTRs. It also impairs Ded1 stimulation of PIC assembly on a structured mRNA in vitro. Ablating Ded1 interactions with eIF4A/eIF4E unveiled a requirement for the Ded1-CTD for robust initiation. Thus, Ded1 function in vivo is stimulated by independent interactions of its NTD with eIF4E and eIF4A, and its CTD with eIF4G. Ded1/Ddx3 RNA helicase eIF4E eIF4A eIF4G translation initiation Medicine R Science Q Biology (General) Neha Gupta verfasserin aut Jon R Lorsch verfasserin aut Alan G Hinnebusch verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.58243 kostenfrei https://doaj.org/article/75675e0e4795445bbe9ffffe87494d14 kostenfrei https://elifesciences.org/articles/58243 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
allfields_unstemmed	10.7554/eLife.58243 doi (DE-627)DOAJ022140395 (DE-599)DOAJ75675e0e4795445bbe9ffffe87494d14 DE-627 ger DE-627 rakwb eng QH301-705.5 Suna Gulay verfasserin aut Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Yeast DEAD-box helicase Ded1 stimulates translation initiation, particularly of mRNAs with structured 5'UTRs. Interactions of the Ded1 N-terminal domain (NTD) with eIF4A, and Ded1-CTD with eIF4G, subunits of eIF4F, enhance Ded1 unwinding activity and stimulation of preinitiation complex (PIC) assembly in vitro. However, the importance of these interactions, and of Ded1-eIF4E association, in vivo were poorly understood. We identified separate amino acid clusters in the Ded1-NTD required for binding to eIF4A or eIF4E in vitro. Disrupting each cluster selectively impairs native Ded1 association with eIF4A or eIF4E, and reduces cell growth, polysome assembly, and translation of reporter mRNAs with structured 5'UTRs. It also impairs Ded1 stimulation of PIC assembly on a structured mRNA in vitro. Ablating Ded1 interactions with eIF4A/eIF4E unveiled a requirement for the Ded1-CTD for robust initiation. Thus, Ded1 function in vivo is stimulated by independent interactions of its NTD with eIF4E and eIF4A, and its CTD with eIF4G. Ded1/Ddx3 RNA helicase eIF4E eIF4A eIF4G translation initiation Medicine R Science Q Biology (General) Neha Gupta verfasserin aut Jon R Lorsch verfasserin aut Alan G Hinnebusch verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.58243 kostenfrei https://doaj.org/article/75675e0e4795445bbe9ffffe87494d14 kostenfrei https://elifesciences.org/articles/58243 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
allfieldsGer	10.7554/eLife.58243 doi (DE-627)DOAJ022140395 (DE-599)DOAJ75675e0e4795445bbe9ffffe87494d14 DE-627 ger DE-627 rakwb eng QH301-705.5 Suna Gulay verfasserin aut Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Yeast DEAD-box helicase Ded1 stimulates translation initiation, particularly of mRNAs with structured 5'UTRs. Interactions of the Ded1 N-terminal domain (NTD) with eIF4A, and Ded1-CTD with eIF4G, subunits of eIF4F, enhance Ded1 unwinding activity and stimulation of preinitiation complex (PIC) assembly in vitro. However, the importance of these interactions, and of Ded1-eIF4E association, in vivo were poorly understood. We identified separate amino acid clusters in the Ded1-NTD required for binding to eIF4A or eIF4E in vitro. Disrupting each cluster selectively impairs native Ded1 association with eIF4A or eIF4E, and reduces cell growth, polysome assembly, and translation of reporter mRNAs with structured 5'UTRs. It also impairs Ded1 stimulation of PIC assembly on a structured mRNA in vitro. Ablating Ded1 interactions with eIF4A/eIF4E unveiled a requirement for the Ded1-CTD for robust initiation. Thus, Ded1 function in vivo is stimulated by independent interactions of its NTD with eIF4E and eIF4A, and its CTD with eIF4G. Ded1/Ddx3 RNA helicase eIF4E eIF4A eIF4G translation initiation Medicine R Science Q Biology (General) Neha Gupta verfasserin aut Jon R Lorsch verfasserin aut Alan G Hinnebusch verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.58243 kostenfrei https://doaj.org/article/75675e0e4795445bbe9ffffe87494d14 kostenfrei https://elifesciences.org/articles/58243 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
allfieldsSound	10.7554/eLife.58243 doi (DE-627)DOAJ022140395 (DE-599)DOAJ75675e0e4795445bbe9ffffe87494d14 DE-627 ger DE-627 rakwb eng QH301-705.5 Suna Gulay verfasserin aut Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Yeast DEAD-box helicase Ded1 stimulates translation initiation, particularly of mRNAs with structured 5'UTRs. Interactions of the Ded1 N-terminal domain (NTD) with eIF4A, and Ded1-CTD with eIF4G, subunits of eIF4F, enhance Ded1 unwinding activity and stimulation of preinitiation complex (PIC) assembly in vitro. However, the importance of these interactions, and of Ded1-eIF4E association, in vivo were poorly understood. We identified separate amino acid clusters in the Ded1-NTD required for binding to eIF4A or eIF4E in vitro. Disrupting each cluster selectively impairs native Ded1 association with eIF4A or eIF4E, and reduces cell growth, polysome assembly, and translation of reporter mRNAs with structured 5'UTRs. It also impairs Ded1 stimulation of PIC assembly on a structured mRNA in vitro. Ablating Ded1 interactions with eIF4A/eIF4E unveiled a requirement for the Ded1-CTD for robust initiation. Thus, Ded1 function in vivo is stimulated by independent interactions of its NTD with eIF4E and eIF4A, and its CTD with eIF4G. Ded1/Ddx3 RNA helicase eIF4E eIF4A eIF4G translation initiation Medicine R Science Q Biology (General) Neha Gupta verfasserin aut Jon R Lorsch verfasserin aut Alan G Hinnebusch verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.58243 kostenfrei https://doaj.org/article/75675e0e4795445bbe9ffffe87494d14 kostenfrei https://elifesciences.org/articles/58243 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
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topic_facet	Ded1/Ddx3 RNA helicase eIF4E eIF4A eIF4G translation initiation Medicine R Science Q Biology (General)
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container_title	eLife
authorswithroles_txt_mv	Suna Gulay @@aut@@ Neha Gupta @@aut@@ Jon R Lorsch @@aut@@ Alan G Hinnebusch @@aut@@
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callnumber-first	Q - Science
author	Suna Gulay
spellingShingle	Suna Gulay misc QH301-705.5 misc Ded1/Ddx3 misc RNA helicase misc eIF4E misc eIF4A misc eIF4G misc translation initiation misc Medicine misc R misc Science misc Q misc Biology (General) Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo
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topic_title	QH301-705.5 Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo Ded1/Ddx3 RNA helicase eIF4E eIF4A eIF4G translation initiation
topic	misc QH301-705.5 misc Ded1/Ddx3 misc RNA helicase misc eIF4E misc eIF4A misc eIF4G misc translation initiation misc Medicine misc R misc Science misc Q misc Biology (General)
topic_unstemmed	misc QH301-705.5 misc Ded1/Ddx3 misc RNA helicase misc eIF4E misc eIF4A misc eIF4G misc translation initiation misc Medicine misc R misc Science misc Q misc Biology (General)
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title	Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo
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title_full	Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo
author_sort	Suna Gulay
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author_browse	Suna Gulay Neha Gupta Jon R Lorsch Alan G Hinnebusch
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title_sort	distinct interactions of eif4a and eif4e with rna helicase ded1 stimulate translation in vivo
callnumber	QH301-705.5
title_auth	Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo
abstract	Yeast DEAD-box helicase Ded1 stimulates translation initiation, particularly of mRNAs with structured 5'UTRs. Interactions of the Ded1 N-terminal domain (NTD) with eIF4A, and Ded1-CTD with eIF4G, subunits of eIF4F, enhance Ded1 unwinding activity and stimulation of preinitiation complex (PIC) assembly in vitro. However, the importance of these interactions, and of Ded1-eIF4E association, in vivo were poorly understood. We identified separate amino acid clusters in the Ded1-NTD required for binding to eIF4A or eIF4E in vitro. Disrupting each cluster selectively impairs native Ded1 association with eIF4A or eIF4E, and reduces cell growth, polysome assembly, and translation of reporter mRNAs with structured 5'UTRs. It also impairs Ded1 stimulation of PIC assembly on a structured mRNA in vitro. Ablating Ded1 interactions with eIF4A/eIF4E unveiled a requirement for the Ded1-CTD for robust initiation. Thus, Ded1 function in vivo is stimulated by independent interactions of its NTD with eIF4E and eIF4A, and its CTD with eIF4G.
abstractGer	Yeast DEAD-box helicase Ded1 stimulates translation initiation, particularly of mRNAs with structured 5'UTRs. Interactions of the Ded1 N-terminal domain (NTD) with eIF4A, and Ded1-CTD with eIF4G, subunits of eIF4F, enhance Ded1 unwinding activity and stimulation of preinitiation complex (PIC) assembly in vitro. However, the importance of these interactions, and of Ded1-eIF4E association, in vivo were poorly understood. We identified separate amino acid clusters in the Ded1-NTD required for binding to eIF4A or eIF4E in vitro. Disrupting each cluster selectively impairs native Ded1 association with eIF4A or eIF4E, and reduces cell growth, polysome assembly, and translation of reporter mRNAs with structured 5'UTRs. It also impairs Ded1 stimulation of PIC assembly on a structured mRNA in vitro. Ablating Ded1 interactions with eIF4A/eIF4E unveiled a requirement for the Ded1-CTD for robust initiation. Thus, Ded1 function in vivo is stimulated by independent interactions of its NTD with eIF4E and eIF4A, and its CTD with eIF4G.
abstract_unstemmed	Yeast DEAD-box helicase Ded1 stimulates translation initiation, particularly of mRNAs with structured 5'UTRs. Interactions of the Ded1 N-terminal domain (NTD) with eIF4A, and Ded1-CTD with eIF4G, subunits of eIF4F, enhance Ded1 unwinding activity and stimulation of preinitiation complex (PIC) assembly in vitro. However, the importance of these interactions, and of Ded1-eIF4E association, in vivo were poorly understood. We identified separate amino acid clusters in the Ded1-NTD required for binding to eIF4A or eIF4E in vitro. Disrupting each cluster selectively impairs native Ded1 association with eIF4A or eIF4E, and reduces cell growth, polysome assembly, and translation of reporter mRNAs with structured 5'UTRs. It also impairs Ded1 stimulation of PIC assembly on a structured mRNA in vitro. Ablating Ded1 interactions with eIF4A/eIF4E unveiled a requirement for the Ded1-CTD for robust initiation. Thus, Ded1 function in vivo is stimulated by independent interactions of its NTD with eIF4E and eIF4A, and its CTD with eIF4G.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
title_short	Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo
url	https://doi.org/10.7554/eLife.58243 https://doaj.org/article/75675e0e4795445bbe9ffffe87494d14 https://elifesciences.org/articles/58243 https://doaj.org/toc/2050-084X
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author2	Neha Gupta Jon R Lorsch Alan G Hinnebusch
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up_date	2024-07-04T00:21:59.293Z
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Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo

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