Literature summary for 3.6.4.13 extracted from

Aryanpur, P.P.; Renner, D.M.; Rodela, E.; Mittelmeier, T.M.; Byrd, A.; Bolger, T.A.
The DEAD-box RNA helicase Ded1 has a role in the translational response to TORC1 inhibition (2019), Mol. Biol. Cell, 30, 2171-2184 .

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O	Saccharomyces cerevisiae	-	ADP + phosphate	-	?
ATP + H2O	Saccharomyces cerevisiae ATCC 204508	-	ADP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P06634	-	-
Saccharomyces cerevisiae ATCC 204508	P06634	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Saccharomyces cerevisiae	ADP + phosphate	-	?
ATP + H2O	-	Saccharomyces cerevisiae ATCC 204508	ADP + phosphate	-	?

Subunits

Subunits	Comment	Organism
More	Ded1 domain structure, the C-terminal domain lies outside of the helicase core domain. It contains TORC1-dependent phosphoserines, and two conserved tryptophans at the C-terminal tail	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
ATP-dependent RNA helicase	-	Saccharomyces cerevisiae
DEAD-box RNA helicase	-	Saccharomyces cerevisiae
DED1	-	Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
malfunction	C-terminal mutants of DED1 are defective in downregulating transxadlation following TORC1 inhibition using rapamycin. EIF4G1 normally dissociates from translation complexes and is degraded, and this process is attenuated in mutant cells. The repressive function of overexpressed Ded1 is partially dependent on the Ded1 C-terminal domain, which is a predicted low-complexity sequence that lies outside of the core helicase domains. Deletion of this domain (amino acids 536-604) substantially rescues growth inhibition on overexpression. Deletion of the Ded1 C-terminus confers resistance against small molecule growth inhibitor rapamycin, a specific inhibitor of TORC1	Saccharomyces cerevisiae
metabolism	Ded1 activity plays an important role in promoting translation repression and adaptation to stress conditions. Ded1 activity is essential for translaxadtion initiation, but above a certain threshold Ded1 becomes inhibitory toward translation	Saccharomyces cerevisiae
additional information	the C-terminal domain of Ded1 (amino acids 536-604) is a low complexity sequence that is necessary for the interaction with eIF4G1 and for self-association and the formation of Ded1 oligomers	Saccharomyces cerevisiae
physiological function	Ded1 is a DEAD-box RNA helicase with essential roles in translation initiation. It binds to the eukaryotic initiation factor 4F (eIF4F) complex and promotes 48S preinitiation complex assembly and start-site scanning of 5' untranslated regions of mRNAs. Role of the enzyme in the translational response during target of rapamycin (TOR)C1 inhibition and function of Ded1 as a translation repressor, overview. Both the rapamycin resistance and impaired survivability following nutrient starvation suggest an important role for the Ded1 C-terminus in the cellular changes that occur during long-term nutrient stress and inhibition of TORC1. Ded1 enzymatic activity and interaction with eIF4G1 are required, while homooligomerization may be dispensable, mapping of the functional requirements for Ded1 in the translaxadtional response. Ded1 stalls translation and specifically removes eIF4G1 from translation preinitiation complexes, thus removing eIF4G1 from the translating mRNA pool and leading to the codegradation of both proteins. The enzyme's role is conserved and may be implicated in pathologies such as oncogenesis	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)