Obese Yeast: Triglyceride Lipolysis Is Functionally Conserved from Mammals to Yeast
| Autor: | Klaus Natter, Harald Scholz, Kim Scheuringer, Robert Zimmermann, Heimo Wolinski, Sepp D. Kohlwein, Regina Leber, Christoph F. Kurat, Julia Petschnigg, Rudolf Zechner |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Lipolysis Molecular Sequence Data Saccharomyces cerevisiae Biology Biochemistry Substrate Specificity Diglycerides Evolution Molecular Mice chemistry.chemical_compound Lipid droplet Animals Amino Acid Sequence Obesity Lipase Molecular Biology Conserved Sequence Triglycerides Mammals Triglyceride lipase Triglyceride Cell Biology biology.organism_classification Yeast Protein Structure Tertiary Kinetics chemistry Mutation Adipose triglyceride lipase biology.protein Patatin |
| Zdroj: | Journal of Biological Chemistry. 281:491-500 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m508414200 |
| Popis: | Storage and degradation of triglycerides are essential processes to ensure energy homeostasis and availability of precursors for membrane lipid synthesis. Recent evidence suggests that an emerging class of enzymes containing a conserved patatin domain are centrally important players in lipid degradation. Here we describe the identification and characterization of a major triglyceride lipase of the adipose triglyceride lipase/Brummer family, Tgl4, in the yeast Saccharomyces cerevisiae. Elimination of Tgl4 in a tgl3 background led to fat yeast, rendering growing cells unable to degrade triglycerides. Tgl4 and Tgl3 lipases localized to lipid droplets, independent of each other. Serine 315 in the GXSXG lipase active site consensus sequence of the patatin domain of Tgl4 is essential for catalytic activity. Mouse adipose triglyceride lipase (which also contains a patatin domain but is otherwise highly divergent in primary structure from any yeast protein) localized to lipid droplets when expressed in yeast, and significantly restored triglyceride breakdown in tgl4 mutants in vivo. Our data identify yeast Tgl4 as a functional ortholog of mammalian adipose triglyceride lipase. |
| Databáze: | OpenAIRE |
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