Thoms, Sven

[["dc.bibliographiccitation.firstpage","504"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The FEBS Journal"],["dc.bibliographiccitation.lastpage","514"],["dc.bibliographiccitation.volume","275"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Debelyy, Mykhaylo O."],["dc.contributor.author","Nau, Katja"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:24:04Z"],["dc.date.available","2020-08-10T05:24:04Z"],["dc.date.issued","2008"],["dc.description.abstract","Lpx1p (systematic name: Yor084wp) is a peroxisomal protein from Saccharomyces cerevisiae with a peroxisomal targeting signal type 1 (PTS1) and a lipase motif. Using mass spectrometry, we have identified Lpx1p as present in peroxisomes, and show that Lpx1p import is dependent on the PTS1 receptor Pex5p. We provide evidence that Lpx1p is piggyback-transported into peroxisomes. We have expressed the Lpx1p protein in Escherichia coli, and show that the enzyme exerts acyl hydrolase and phospholipase A activity in vitro. However, the protein is not required for wild-type-like steady-state function of peroxisomes, which might be indicative of a metabolic rather than a biogenetic role. Interestingly, peroxisomes in deletion mutants of LPX1 have an aberrant morphology characterized by intraperoxisomal vesicles or invaginations."],["dc.identifier.doi","10.1111/j.1742-4658.2007.06217.x"],["dc.identifier.pmid","18199283"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67542"],["dc.language.iso","en"],["dc.relation.issn","1742-464X"],["dc.title","Lpx1p is a peroxisomal lipase required for normal peroxisome morphology"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","770"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Eukaryotic Cell"],["dc.bibliographiccitation.lastpage","775"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Debelyy, Mykhaylo O."],["dc.contributor.author","Connerth, Melanie"],["dc.contributor.author","Daum, Günther"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:59:18Z"],["dc.date.available","2020-08-10T05:59:18Z"],["dc.date.issued","2011"],["dc.description.abstract","Here, we report the identification of a novel hydrolase in Saccharomyces cerevisiae. Ldh1p (systematic name, Ybr204cp) comprises the typical GXSXG-type lipase motif of members of the α/β-hydrolase family and shares some features with the peroxisomal lipase Lpx1p. Both proteins carry a putative peroxisomal targeting signal type1 (PTS1) and can be aligned with two regions of homology. While Lpx1p is known as a peroxisomal enzyme, subcellular localization studies revealed that Ldh1p is predominantly localized to lipid droplets, the storage compartment of nonpolar lipids. Ldh1p is not required for the function and biogenesis of peroxisomes, and targeting of Ldh1p to lipid droplets occurs independently of the PTS1 receptor Pex5p."],["dc.identifier.doi","10.1128/EC.05038-11"],["dc.identifier.pmid","21478430"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67554"],["dc.language.iso","en"],["dc.relation.eissn","1535-9786"],["dc.relation.issn","1535-9778"],["dc.title","The putative Saccharomyces cerevisiae hydrolase Ldh1p is localized to lipid droplets"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","776"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Eukaryotic Cell"],["dc.bibliographiccitation.lastpage","781"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Debelyy, Mykhaylo O."],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Connerth, Melanie"],["dc.contributor.author","Daum, Günther"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:17:53Z"],["dc.date.available","2020-08-10T05:17:53Z"],["dc.date.issued","2011"],["dc.description.abstract","Here, we report the functional characterization of the newly identified lipid droplet hydrolase Ldh1p. Recombinant Ldh1p exhibits esterase and triacylglycerol lipase activities. Mutation of the serine in the hydrolase/lipase motif GXSXG completely abolished esterase activity. Ldh1p is required for the maintenance of a steady-state level of the nonpolar and polar lipids of lipid droplets. A characteristic feature of the Saccharomyces cerevisiae Δldh1 strain is the appearance of giant lipid droplets and an excessive accumulation of nonpolar lipids and phospholipids upon growth on medium containing oleic acid as a sole carbon source. Ldh1p is thought to play a role in maintaining the lipid homeostasis in yeast by regulating both phospholipid and nonpolar lipid levels."],["dc.identifier.doi","10.1128/EC.05040-11"],["dc.identifier.pmid","21478434"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67539"],["dc.language.iso","en"],["dc.relation.eissn","1535-9786"],["dc.relation.issn","1535-9778"],["dc.title","Involvement of the Saccharomyces cerevisiae hydrolase Ldh1p in lipid homeostasis"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","28223"],["dc.bibliographiccitation.issue","32"],["dc.bibliographiccitation.journal","The Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","28234"],["dc.bibliographiccitation.volume","286"],["dc.contributor.author","Debelyy, Mykhaylo O."],["dc.contributor.author","Platta, Harald W."],["dc.contributor.author","Saffian, Delia"],["dc.contributor.author","Hensel, Astrid"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","Girzalsky, Wolfgang"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:15:59Z"],["dc.date.available","2020-08-10T05:15:59Z"],["dc.date.issued","2011"],["dc.description.abstract","Peroxisomal matrix protein import is facilitated by cycling receptors shuttling between the cytosol and the peroxisomal membrane. One crucial step in this cycle is the ATP-dependent release of the receptors from the peroxisomal membrane. This step is facilitated by the peroxisomal AAA (ATPases associated with various cellular activities) proteins Pex1p and Pex6p with ubiquitination of the receptor being the main signal for its export. Here we report that the AAA complex contains dislocase as well as deubiquitinating activity. Ubp15p, a ubiquitin hydrolase, was identified as a novel constituent of the complex. Ubp15p partially localizes to peroxisomes and is capable of cleaving off ubiquitin moieties from the type I peroxisomal targeting sequence (PTS1) receptor Pex5p. Furthermore, Ubp15p-deficient cells are characterized by a stress-related PTS1 import defect. The results merge into a picture in which removal of ubiquitin from the PTS1 receptor Pex5p is a specific event and might represent a vital step in receptor recycling."],["dc.identifier.doi","10.1074/jbc.M111.238600"],["dc.identifier.pmid","21665945"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67538"],["dc.language.iso","en"],["dc.relation.eissn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","Ubp15p, a ubiquitin hydrolase associated with the peroxisomal export machinery"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]