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Two yeast enzymes, Psd1p and Psd2p, catalyze the decarboxylation of phosphatidylserine to produce phosphatidylethanolamine (PtdEtn). Mitochondrial Psd1p provides ∼90% of total cellular phosphatidylserine decarboxylase activity. When thePSD1 gene is deleted, the resultant strain(psd1Δ) grows normally at 30 °C in glucose and in the absence of exogenous choline or ethanolamine. However, at elevated temperature (37 °C) or on the nonfermentable carbon source lactate, the growth of psd1Δ strains is minimal without ethanolamine supplementation. The reduced growth and viability correlate with a PtdEtn content below 4% of total phospholipid. These results suggest that there is a critical level of PtdEtn required to support growth. This theory is supported by growth data revealing that a psd1Δ psd2Δ dpl1Δ strain can only grow in the presence of ethanolamine. In contrast, a psd1Δ psd2Δ strain, which makes …