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Transcriptional Response to Deletion of the Phosphatidylserine Decarboxylase Psd1p in the Yeast Saccharomyces cerevisiae
Author(s) -
Martina Gsell,
Gerald Mascher,
Irmgard Schuiki,
Birgit Ploier,
Claudia Hrastnik,
Günther Daum
Publication year - 2013
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0077380
Subject(s) - phosphatidylserine , saccharomyces cerevisiae , phosphatidylethanolamine , biology , mutant , gene , microbiology and biotechnology , biochemistry , phospholipid , phosphatidylcholine , membrane
In the yeast, Saccharomyces cerevisiae , the synthesis of the essential phospholipid phosphatidylethanolamine (PE) is accomplished by a network of reactions which comprises four different pathways. The enzyme contributing most to PE formation is the mitochondrial phosphatidylserine decarboxylase 1 (Psd1p) which catalyzes conversion of phosphatidylserine (PS) to PE. To study the genome wide effect of an unbalanced cellular and mitochondrial PE level and in particular the contribution of Psd1p to this depletion we performed a DNA microarray analysis with a ∆ psd1 deletion mutant. This approach revealed that 54 yeast genes were significantly up-regulated in the absence of PSD1 compared to wild type. Surprisingly, marked down-regulation of genes was not observed. A number of different cellular processes in different subcellular compartments were affected in a ∆ psd1 mutant. Deletion mutants bearing defects in all 54 candidate genes, respectively, were analyzed for their growth phenotype and their phospholipid profile. Only three mutants, namely ∆ gpm2 , ∆ gph1 and ∆ rsb1 , were affected in one of these parameters. The possible link of these mutations to PE deficiency and PSD1 deletion is discussed.

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