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dc.date.accessioned2018-08-20T15:55:58Z
dc.date.available2018-08-20T15:55:58Z
dc.date.issued2018-07-11
dc.identifier.issn2218-273X
dc.identifier.uriurn:nbn:de:hebis:34-2018082056192
dc.identifier.urihttp://hdl.handle.net/123456789/2018082056192
dc.description.sponsorshipGefördert durch den Publikationsfonds der Universität Kassel
dc.language.isoeng
dc.subjectsoraphen Aeng
dc.subjectSit4eng
dc.subjecttRNA modificationeng
dc.subjectElongator complexeng
dc.subject.ddc570
dc.titleProtein Phosphatase Sit4 Affects Lipid Droplet Synthesis and Soraphen A Resistance Independent of Its Role in Regulating Elongator Dependent tRNA Modificationeng
dc.typeAufsatz
dcterms.abstractThe 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.eng
dcterms.accessRightsopen access
dcterms.bibliographicCitationIn: Biomolecules. - Basel : MDPI. - 2018, 8(3), 49, 1-12
dcterms.creatorBozaquel-Morais, Bruno Leonardo
dcterms.creatorVogt, Leonie
dcterms.creatorD’Angelo, Valentina
dcterms.creatorSchaffrath, Raffael
dcterms.creatorKlassen, Roland
dcterms.creatorMontero-Lomelí, Mónica
dc.relation.doidoi:10.3390/biom8030049


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