Date
2023-10-21Author
Soares Matos, GabrielVogt, LeonieSilva Santos, RosangelaDevillars, AurélienYoshinaga, Marcos YukioMiyamoto, SayuriSchaffrath, RaffaelMontero-Lomeli, MonicaKlassen, RolandMetadata
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Aufsatz
Lipidome remodeling in response to nutrient replenishment requires the tRNA modifier Deg1/Pus3 in yeast
Abstract
In 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.
Citation
In: Molecular Microbiology Volume 120 / Issue 6 (2023-10-21) , S. 893-905 ; eissn:1365-2958Sponsorship
Gefördert im Rahmen des Projekts DEALCitation
@article{doi:10.17170/kobra-202312209252,
author={Soares Matos, Gabriel and Vogt, Leonie and Silva Santos, Rosangela and Devillars, Aurélien and Yoshinaga, Marcos Yukio and Miyamoto, Sayuri and Schaffrath, Raffael and Montero-Lomeli, Monica and Klassen, Roland},
title={Lipidome remodeling in response to nutrient replenishment requires the tRNA modifier Deg1/Pus3 in yeast},
journal={Molecular Microbiology},
year={2023}
}
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2024-02-12T15:35:07Z 2024-02-12T15:35:07Z 2023-10-21 doi:10.17170/kobra-202312209252 http://hdl.handle.net/123456789/15454 Gefördert im Rahmen des Projekts DEAL eng Namensnennung 4.0 International http://creativecommons.org/licenses/by/4.0/ liqid droplets lipidome pseudouridine storage lipids tRNA yeast 570 Lipidome remodeling in response to nutrient replenishment requires the tRNA modifier Deg1/Pus3 in yeast Aufsatz In 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. open access Soares Matos, Gabriel Vogt, Leonie Silva Santos, Rosangela Devillars, Aurélien Yoshinaga, Marcos Yukio Miyamoto, Sayuri Schaffrath, Raffael Montero-Lomeli, Monica Klassen, Roland doi:10.1111/mmi.15185 Grant 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 Pseudouridin Lipidstoffwechsel Transfer-RNS Bäckerhefe publishedVersion eissn:1365-2958 Issue 6 Molecular Microbiology 893-905 Volume 120 false
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