Literature summary for 2.5.1.46 extracted from

Galvao, F.C.; Rossi, D.; Silveira, W.d.a..S.; Valentini, S.R.; Zanelli, C.F.
The deoxyhypusine synthase mutant dys1-1 reveals the association of eIF5A and Asc1 with cell wall integrity (2013), PLoS ONE, 8, e60140.

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Protein Variants

Protein Variants	Comment	Organism
additional information	generation of the dys1-1 mutant that has a defect in total protein synthesis, a defect in polysome profile indicative of a translation elongation defect and a reduced association of eIF5A with polysomes	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
[eIF5A-precursor]-lysine + spermidine	Saccharomyces cerevisiae	-	[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
[eIF5A-precursor]-lysine + spermidine	-	Saccharomyces cerevisiae	[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine	-	?

Synonyms

Synonyms	Comment	Organism
Dys1	-	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
malfunction	the dys1-1 mutant shows a strong depletion of mutated Dys1 protein, resulting in more than 2fold decrease in hypusine levels relative to the wild type. he growth phenotype of dys1-1 mutant is severe, growing only in the presence of 1 M sorbitol, an osmotic stabilizer, the sorbitol requirement from dys1-1 is not associated with cell lysis. The dys1-1 mutant genetically interacts with the sole yeast protein kinase C (Pkc1) and Asc1, a component of the 40S ribosomal subunit. The dys1-1 mutant is synthetically lethal in combination with asc1DELTA and overexpression of TIF51A (eIF5A) or DYS1 is toxic for an asc1DELTA strain. Inactive Pkc1 (K853R) form does not affect the dys1-1 mutant. Dys1-1 mutant phenotype, overview	Saccharomyces cerevisiae
metabolism	the functions of Asc1 associated with protein synthesis are necessary in the absence of wild type levels of hypusine-containing eIF5A in the cell	Saccharomyces cerevisiae
physiological function	translation factor eIF5A undergoes an essential and conserved posttranslational modification at a specific lysine, K51, to generate the residue hypusine. The enzymes deoxyhypusine synthase (Dys1) and deoxyhypusine hydroxylase (Lia1) catalyze this two-step modification process. Correlated role for eIF5A and Asc1 in coordinating the translational control of a subset of mRNAs associated with cell integrity	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)