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2) Sollner, S.; Nebauer, R.; Ehammer, H.; Prem, A.; Deller, S.; Palfey, B. A.; Daum, G. and Macheroux, P. Lot6p from Saccharomyces cerevisiae is a FMN-dependent reductase with a potential role in quinone detoxification FEBS J. 274 (2007) 1328-1339 3) Czabany, T., Athenstaedt, K. and Daum, G. Synthesis, storage and degradation of neutral lipids in yeast Biochim. Biophys. Acta 1771 (2007) 299-309 4) Wriessnegger, T, Gübitz, G, Leitner, E, Ingolic, E, Cregg, J, de la Cruz, B. J. and Daum, G. Lipid composition of peroxisomes from the yeast Pichia pastoris grown on different carbon sources Biochim. Biophys. Acta 1771 (2007) 455-461 5) Perktold, A., Zechmann, B., Daum, G. and Zellnig, G. Organelle association visualized by three-dimensional ultrastructural imaging of the yeast cell FEMS Yeast Research 7(2007) 629-638 6) Nebauer, R., Rosenberger, S. and Daum, G. Phosphatidylethanolamine, a limiting factor of autophagy in yeast strains bearing a defect in the carboxypeptidase y pathway of vacuolar targeting J. Biol. Chem. 282 (2007) 16736-16743 7) Nebauer, R, Schuiki, I., Kulterer, B., Trajanoski, Z. and Daum, G. The phosphatidylethanolamine level of yeast mitochondria is affected by the mitochondrial components Oxa1p and Yme1p FEBS J. 274 (2007) 6180-6190 8) Daum, G, Wagner, A., Czabany, T, Grillitsch, K. and Athenstaedt, K. Lipid storage and mobilization pathways in yeast Novartis Foundation Symposium No.286 (2007), 142-154 Award Ruth Nebauer, a former PhD student, received the Best Paper Award 2006/07 for doctoral students of the Key Research Area “Life Science Technology” of the Graz University of Technology (July 2007) 22
Molecular Biology Group Karin Athenstaedt Lipid particles – more than simple storage compartments (Professorial dissertation) Lipid particles are intracellular compartments consisting of a neutral lipid core surrounded by a phospholipid monolayer with few proteins embedded. In former days, the only function ascribed to these particles was that of a simple storage compartment containing backup molecules, mainly triacylglycerols and steryl esters, which are mobilized when nutrients are no longer provided by the environment. This view, however, had to be revised, since investigations during the last decade demonstrated active participation of lipid particle proteins in lipid metabolism. My work deals with identification and characterization of several lipid particle proteins of the yeast Saccharomyces cerevisiae which are involved in processes such as phosphatidic acid biosynthesis, triacylglycerol and sterol formation, and triacylglycerol mobilization. Analysis of the lipid particle proteome of the oleaginous yeast Yarrowia lipolytica revealed that most proteins are counterparts of lipid particle polypeptides of Saccharomyces cerevisiae. Comparison of the yeasts’ lipid particle proteome with that of higher eukaryotic cells indicates that participation in lipid metabolism is a general feature of this compartment. Is Nte1p of Saccharomyces cerevisiae a true member of the NTE1-family Neuropathy target esterase (NTE) was originally identified as the target of organophosphorous esters (OP) present in many pesticides as well as warfare agents. Toxifications with OPs are causing delayed neuropathy in man and some other vertebrates. The syndrome of the organophosphorous-induced delayed neuropathy (OPIDN) is characterised by paralysis of the lower limbs and degeneration of long axons in the spinal cord. These effects are common responses of neurons in metabolic disorders (e.g., diabetes), toxic states and advanced age. Neither NTE nor its homologs in other organisms are closely related to any other esterase or protease. The importance of NTE can be seen by the fact that mice lacking this protein die as early embryos, and Figure 1: “Holes” in the brain of a sws-mutant of the fruit fly Drosophila melanogaster. First “holes” in the brain of a sws-mutant can be already observed after 5 days (B). The number of “holes” increases progressively with age (20d; C). In contrast, no “holes” can be observed in wild-type brains after 20 days (A). 23
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