Lipidome remodeling in response to nutrient replenishment requires the tRNA modifier Deg1/Pus3 in yeast

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dc.date.accessioned2024-02-12T15:35:07Z
dc.date.available2024-02-12T15:35:07Z
dc.date.issued2023-10-21
dc.description.sponsorshipGefördert im Rahmen des Projekts DEALger
dc.identifierdoi:10.17170/kobra-202312209252
dc.identifier.urihttp://hdl.handle.net/123456789/15454
dc.language.isoeng
dc.relation.doidoi:10.1111/mmi.15185
dc.relation.projectidGrant Numbers: KL2937/1, SCHA750/18, SCHA750/19, SCHA750/20 ; Grant Numbers: E26/201.070/2021, E26/210446/2019 ; Grant Numbers: CEPID-Redoxoma 13/07937-8, CNPq 313926/2021-2
dc.rightsNamensnennung 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectliqid dropletseng
dc.subjectlipidomeeng
dc.subjectpseudouridineeng
dc.subjectstorage lipidseng
dc.subjecttRNAeng
dc.subjectyeasteng
dc.subject.ddc570
dc.subject.swdPseudouridinger
dc.subject.swdLipidstoffwechselger
dc.subject.swdTransfer-RNSger
dc.subject.swdBäckerhefeger
dc.titleLipidome remodeling in response to nutrient replenishment requires the tRNA modifier Deg1/Pus3 in yeasteng
dc.typeAufsatz
dc.type.versionpublishedVersion
dcterms.abstractIn the yeast Saccharomyces cerevisiae, the absence of the pseudouridine synthase Pus3/Deg1, which modifies tRNA positions 38 and 39, results in increased lipid droplet (LD) content and translational defects. In addition, starvation-like transcriptome alterations and induced protein aggregation were observed. In this study, we show that the deg1 mutant increases specific misreading errors. This could lead to altered expression of the main regulators of neutral lipid synthesis which are the acetyl-CoA carboxylase (Acc1), an enzyme that catalyzes a key step in fatty acid synthesis, and its regulator, the Snf1/AMPK kinase. We demonstrate that upregulation of the neutral lipid content of LD in the deg1 mutant is achieved by a mechanism operating in parallel to the known Snf1/AMPK kinase-dependent phosphoregulation of Acc1. While in wild-type cells removal of the regulatory phosphorylation site (Ser-1157) in Acc1 results in strong upregulation of triacylglycerol (TG), but not steryl esters (SE), the deg1 mutation more specifically upregulates SE levels. In order to elucidate if other lipid species are affected, we compared the lipidomes of wild type and deg1 mutants, revealing multiple altered lipid species. In particular, in the exponential phase of growth, the deg1 mutant shows a reduction in the pool of phospholipids, indicating a compromised capacity to mobilize acyl-CoA from storage lipids. We conclude that Deg1 plays a key role in the coordination of lipid storage and mobilization, which in turn influences lipid homeostasis. The lipidomic effects in the deg1 mutant may be indirect outcomes of the activation of various stress responses resulting from protein aggregation.eng
dcterms.accessRightsopen access
dcterms.creatorSoares Matos, Gabriel
dcterms.creatorVogt, Leonie
dcterms.creatorSilva Santos, Rosangela
dcterms.creatorDevillars, Aurélien
dcterms.creatorYoshinaga, Marcos Yukio
dcterms.creatorMiyamoto, Sayuri
dcterms.creatorSchaffrath, Raffael
dcterms.creatorMontero-Lomeli, Monica
dcterms.creatorKlassen, Roland
dcterms.source.identifiereissn:1365-2958
dcterms.source.issueIssue 6
dcterms.source.journalMolecular Microbiologyeng
dcterms.source.pageinfo893-905
dcterms.source.volumeVolume 120
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