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Regulation of the PAH1‐encoded phosphatidate phosphatase during lipogenesis in the oleaginous yeast Yarrowia lipolytica
Author(s) -
Carmon Taylor,
Ukey Rahul,
Fakas Stylianos
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.05295
Subject(s) - phosphatidate , lipogenesis , diacylglycerol kinase , biochemistry , yarrowia , chemistry , yeast , gene , enzyme , protein kinase c
The PAH 1 gene encodes for phosphatidate phosphatase (PAP) that plays a vital role in lipid biosynthesis by catalyzing the conversion of phosphatidate (PA) to diacylglycerol (DAG) which is used to synthesize triacylglycerol (TAG). Previous research has shown that PAP activity is elevated during growth in media that induce lipogenesis. In this work, the PAH1 ‐encoded PAP activity and protein levels were analyzed in wild type and pah1 Δ cells during lipogenesis. The results showed that the PAH1 ‐encoded PAP activity increased in a time‐dependent manner, but the Pah1 levels declined with time. Examination of the subcellular fractions revealed that Pah1 was almost entirely responsible for the membrane‐associated PAP activity. The lipid content of the wild type cells was higher than that of the pah1 Δ cells, while the pah1 Δ mutation did not have a major effect on the levels of DAG and TAG. Support or Funding Information This work was supported, in whole or in part, by National Institutes of Health Grant R15GM124602‐01 from the United States Public Health Service. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.