University Archives

Putative 2-methylcitrate dehydratase (PDH1) is a Saccharomyces cerevisiae mitochondrial protein that participates in propionate metabolism. The PDH1 gene in Saccharomyces cerevisiae is orthologous to the human gene aconitate decarboxylase 1 (ACOD1), which recent reports suggest is a regulator of immunometabolism in inflammation and infection. However, the metabolic consequences of PDH1 deletion have not yet been fully characterized. To further explore the molecular functions of PDH1, we performed liquid chromatography-mass spectrometry (LC-MS)-based metabolomics to compare PDH1 deletion mutant yeast to BY4741 wild-type yeast. Both intracellular and extracellular metabolite extractions were performed on yeast cultures harvested at mid-log growth phase. The yeast extracts were analyzed by reversed-phase chromatography coupled to a time-of-flight mass spectrometer operated in positive ionization mode. Following untargeted feature detection and alignment, univariate and multivariate statistical analysis were performed to detect differential features between the yeast strains. Putative compound identification was performed by matching accurate mass to literature databases. Preliminary results, which suggest the mutation has multiple potential metabolic effects, will be described.