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2018-07-11Author
Bozaquel-Morais, Bruno LeonardoVogt, LeonieD’Angelo, ValentinaSchaffrath, RaffaelKlassen, RolandMontero-Lomelí, MónicaSubject
570 Life sciences; biologyMetadata
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Artikel (Publikationen im Open Access gefördert durch die UB)
Protein Phosphatase Sit4 Affects Lipid Droplet Synthesis and Soraphen A Resistance Independent of Its Role in Regulating Elongator Dependent tRNA Modification
Abstract
The protein phosphatase Sit4 has been shown to be required for lipogenesis and resistance against the acetyl-CoA carboxylase inhibitor soraphen A. Since Sit4 is also required for biosynthesis of Elongator dependent tRNA modifications such as 5-methoxycarbonylmethyluridine (mcm5U), we investigated the relevance of tRNA modifications in lipogenesis and soraphen A response. While sit4 and Elongator (elp3) mutants copy defects in mcm5U formation and stress sensitivity, they do not share soraphen A sensitivity and low lipid droplet (LD) phenotypes. In contrast to sit4, we found elp3 mutants to display partial soraphen A resistance and a high LD phenotype. Screening a collection of tRNA modification mutants additionally identified the tRNA pseudo-uridine synthase gene DEG1 to be required for soraphen A sensitivity. Since deg1 and elp3 share high LD and soraphen A resistance phenotypes, these are likely caused by translational defects. In support of this notion, we observe overexpression of tRNAGlnUUG suppresses lipolysis defects of deg1 mutants. Hence, the sit4 mutation results in a composite defect including tRNA modification deficiency and loss of Snf1 kinase dephosphorylation, which induce opposite effects on LD regulation. Importantly, however, the Snf1 kinase regulatory defects of the phosphatase mutant dominate over effects on LD regulation imposed by loss of the tRNA modification alone.
Citation
In: Biomolecules. - Basel : MDPI. - 2018, 8(3), 49, 1-12Sponsorship
Gefördert durch den Publikationsfonds der Universität KasselCollections
Publikationen (Fachgebiet Mikrobiologie)Artikel (Publikationen im Open Access gefördert durch die UB)
Citation
@article{urn:nbn:de:hebis:34-2018082056192,
author={Bozaquel-Morais, Bruno Leonardo and Vogt, Leonie and D’Angelo, Valentina and Schaffrath, Raffael and Klassen, Roland and Montero-Lomelí, Mónica},
title={Protein Phosphatase Sit4 Affects Lipid Droplet Synthesis and Soraphen A Resistance Independent of Its Role in Regulating Elongator Dependent tRNA Modification},
year={2018}
}
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2018-08-20T15:55:58Z 2018-08-20T15:55:58Z 2018-07-11 2218-273X urn:nbn:de:hebis:34-2018082056192 http://hdl.handle.net/123456789/2018082056192 Gefördert durch den Publikationsfonds der Universität Kassel eng Urheberrechtlich geschützt https://rightsstatements.org/page/InC/1.0/ soraphen A Sit4 tRNA modification Elongator complex 570 Protein Phosphatase Sit4 Affects Lipid Droplet Synthesis and Soraphen A Resistance Independent of Its Role in Regulating Elongator Dependent tRNA Modification Aufsatz The protein phosphatase Sit4 has been shown to be required for lipogenesis and resistance against the acetyl-CoA carboxylase inhibitor soraphen A. Since Sit4 is also required for biosynthesis of Elongator dependent tRNA modifications such as 5-methoxycarbonylmethyluridine (mcm5U), we investigated the relevance of tRNA modifications in lipogenesis and soraphen A response. While sit4 and Elongator (elp3) mutants copy defects in mcm5U formation and stress sensitivity, they do not share soraphen A sensitivity and low lipid droplet (LD) phenotypes. In contrast to sit4, we found elp3 mutants to display partial soraphen A resistance and a high LD phenotype. Screening a collection of tRNA modification mutants additionally identified the tRNA pseudo-uridine synthase gene DEG1 to be required for soraphen A sensitivity. Since deg1 and elp3 share high LD and soraphen A resistance phenotypes, these are likely caused by translational defects. In support of this notion, we observe overexpression of tRNAGlnUUG suppresses lipolysis defects of deg1 mutants. Hence, the sit4 mutation results in a composite defect including tRNA modification deficiency and loss of Snf1 kinase dephosphorylation, which induce opposite effects on LD regulation. Importantly, however, the Snf1 kinase regulatory defects of the phosphatase mutant dominate over effects on LD regulation imposed by loss of the tRNA modification alone. open access In: Biomolecules. - Basel : MDPI. - 2018, 8(3), 49, 1-12 Bozaquel-Morais, Bruno Leonardo Vogt, Leonie D’Angelo, Valentina Schaffrath, Raffael Klassen, Roland Montero-Lomelí, Mónica doi:10.3390/biom8030049
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