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

DEAD-box RNA Helicases / chemistry Eukaryotic Initiation Factor-4E / chemistry Eukaryotic Initiation Factor-4F / chemistry Gene Expression Regulation, Fungal Polyribosomes / genetics Protein Binding Protein Biosynthesis Protein Domains RNA Helicases / chemistry Saccharomyces cerevisiae / chemistry Saccharomyces cerevisiae Proteins / chemistry
Ded1/Ddx3 RNA helicase S. cerevisiae chromosomes eIF4A eIF4E eIF4G gene expression translation initiation

Journal

eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614

Informations de publication

Date de publication:
29 05 2020
Historique:
received: 24 04 2020
accepted: 28 05 2020
pubmed: 30 5 2020
medline: 19 3 2021
entrez: 30 5 2020
Statut: epublish

Résumé

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.

Identifiants

DOI: 10.7554/eLife.58243 PMID: 32469309 PMC: PMC7343385
pubmed: 32469309
doi: 10.7554/eLife.58243
pii: 58243
pmc: PMC7343385
doi:
pii:

Substances chimiques

Eukaryotic Initiation Factor-4E 0
Eukaryotic Initiation Factor-4F 0
Saccharomyces cerevisiae Proteins 0
DED1 protein, S cerevisiae EC 3.6.1.-
DEAD-box RNA Helicases EC 3.6.4.13
RNA Helicases EC 3.6.4.13
TIF1 protein, S cerevisiae EC 3.6.4.13

Types de publication

Journal Article Research Support, N.I.H., Intramural

Langues

eng

Sous-ensembles de citation

IM

Déclaration de conflit d'intérêts

SG, NG, JL No competing interests declared, AH Reviewing editor, eLife

Références

Science. 1997 Mar 7;275(5305):1468-71
pubmed: 9045610
EMBO J. 2011 Jan 19;30(2):302-16
pubmed: 21139564
Mol Cell. 2015 Aug 20;59(4):541-52
pubmed: 26212457
Methods Enzymol. 1987;154:164-75
pubmed: 3323810
Proc Natl Acad Sci U S A. 1997 May 13;94(10):5201-6
pubmed: 9144215
Nucleic Acids Res. 2019 Sep 19;47(16):8785-8806
pubmed: 31299079
Methods Enzymol. 2007;430:111-45
pubmed: 17913637
Elife. 2016 Aug 05;5:
pubmed: 27494274
Mol Cell. 2010 Sep 24;39(6):950-62
pubmed: 20864040
Nucleic Acids Res. 1989 Aug 11;17(15):5923-31
pubmed: 2671936
Mol Biol Cell. 2019 Aug 1;30(17):2171-2184
pubmed: 31141444
EMBO J. 2001 Feb 15;20(4):891-904
pubmed: 11179233
Oncogene. 2008 Jan 24;27(5):700-14
pubmed: 17667941
RNA Biol. 2017 Feb;14(2):188-196
pubmed: 27981882
RNA. 2002 Mar;8(3):382-97
pubmed: 12008673
Mol Cell Biol. 2010 Sep;30(18):4415-34
pubmed: 20584985
Mol Cell Biol. 1999 Aug;19(8):5557-64
pubmed: 10409745
Nucleic Acids Res. 2014 Sep;42(15):10005-22
pubmed: 25013175
Gene. 1988 Dec 30;74(2):527-34
pubmed: 3073106
Crit Rev Biochem Mol Biol. 2014 Jul-Aug;49(4):343-60
pubmed: 25039764
Mol Cell Biol. 2005 Nov;25(22):9859-73
pubmed: 16260602
Cell Cycle. 2012 Jul 15;11(14):2594-9
pubmed: 22767211
J Biol Chem. 2013 Jan 25;288(4):2340-54
pubmed: 23184954
J Biol Chem. 2016 Jan 29;291(5):2412-21
pubmed: 26598523
J Biol Chem. 1982 Nov 10;257(21):13056-61
pubmed: 6290491
Mol Microbiol. 2002 Oct;46(2):531-44
pubmed: 12406227
Mol Cell. 2011 Sep 16;43(6):962-72
pubmed: 21925384
Elife. 2018 Oct 03;7:
pubmed: 30281017
Annu Rev Biochem. 2014;83:779-812
pubmed: 24499181
Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3889-94
pubmed: 12660367
Genome Res. 2015 Aug;25(8):1196-205
pubmed: 26122911
EMBO J. 1996 Dec 16;15(24):7168-77
pubmed: 9003792
PLoS Genet. 2018 Dec 7;14(12):e1007806
pubmed: 30532217
PLoS One. 2010 Feb 09;5(2):e9114
pubmed: 20161741
Elife. 2017 Nov 30;6:
pubmed: 29192585
Nat Rev Mol Cell Biol. 2010 Feb;11(2):113-27
pubmed: 20094052

Auteurs

Suna Gulay (S)

Division of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, United States.
ORCID: 0000-0002-4672-144X

Neha Gupta (N)

Division of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, United States.

Jon R Lorsch (JR)

Division of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, United States.
ORCID: 0000-0002-4521-4999

Alan G Hinnebusch (AG)

Division of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, United States.
ORCID: 0000-0002-1627-8395

Articles similaires

Exploring structural diversity across the protein universe with The Encyclopedia of Domains.

Andy M Lau, Nicola Bordin, Shaun M Kandathil et al.
1.00
Databases, Protein Protein Domains Protein Folding Proteins Deep Learning

Membrane potential stimulates ADP import and ATP export by the mitochondrial ADP/ATP carrier due to its positively charged binding site.

Vasiliki Mavridou, Martin S King, Andre Bazzone et al.
1.00
Adenosine Triphosphate Adenosine Diphosphate Mitochondrial ADP, ATP Translocases Binding Sites Mitochondria

Menthol as an effective inhibitor of quorum sensing and biofilm formation in Candida albicans and Candida glabrata by targeting the transcriptional repressor TUP1.

Pouria Khodavandi, Maryam Miri Soogh, Fahimeh Alizadeh et al.
1.00
Biofilms Candida albicans Quorum Sensing Candida glabrata Menthol

Conservation of the cooling agent binding pocket within the TRPM subfamily.

Kate Huffer, Matthew C S Denley, Elisabeth V Oskoui et al.
1.00
TRPM Cation Channels Animals Binding Sites Mice Pyrimidinones

Classifications MeSH

questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › Phosphotransferases › Nucleotidyltransferases › RNA nucleotidyltransferases › RNA helicases › DEAD-box RNA helicases › Distinct interactions of eIF4A and eIF4E with...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines ribosomiques › Facteurs initiation chaîne peptidique › Facteurs d'initiation eucaryotes › Facteur-4F d'initiation eucaryote › Facteur-4E d'initiation eucaryote › Distinct interactions of eIF4A and eIF4E with...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines ribosomiques › Facteurs initiation chaîne peptidique › Facteurs d'initiation eucaryotes › Facteur-4F d'initiation eucaryote › Distinct interactions of eIF4A and eIF4E with...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Régulation de l'expression des gènes fongiques › Distinct interactions of eIF4A and eIF4E with...
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Ribosomes › Polyribosomes › Distinct interactions of eIF4A and eIF4E with...
questionsmedicales.fr › Métabolisme › Liaison aux protéines › Distinct interactions of eIF4A and eIF4E with...
questionsmedicales.fr › Phénomènes génétiques › Expression des gènes › Biosynthèse des protéines › Distinct interactions of eIF4A and eIF4E with...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure tertiaire des protéines › Domaines protéiques › Distinct interactions of eIF4A and eIF4E with...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › Phosphotransferases › Nucleotidyltransferases › RNA nucleotidyltransferases › RNA helicases › Distinct interactions of eIF4A and eIF4E with...
questionsmedicales.fr › Eucaryotes › Champignons › Levures › Saccharomyces › Saccharomyces cerevisiae › Distinct interactions of eIF4A and eIF4E with...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines fongiques › Protéines de Saccharomyces cerevisiae › Distinct interactions of eIF4A and eIF4E with...