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J. Biochem, 2003, Vol. 133, No. 4 515-522
© 2003 Japanese Biochemical Society


BIOCHEMISTRY

Role of the Yeast VAP Homolog, Scs2p, in INO1 Expression and Phospholipid Metabolism

Satoshi Kagiwada+ and Rie Zen

Department of Biological Science, Faculty of Science, Nara Women’s University, Nara 630-8506

In the yeast Saccharomyces cerevisiae, the expression of phospholipid biosynthetic genes, including the INO1 gene (encoding inositol-1-phosphate synthase), is coordinately regulated by a cis-acting transcriptional element, UASINO (inositol-sensitive upstream activating sequence). For this paper we studied the effect of SCS2 disruption on INO1 expression. SCS2 encodes a type II membrane protein and its deletion leads to inositol auxotrophy at temperatures above 34°C. We found that the expression of the INO1 gene was reduced in the scs2{Delta} strain even when the cells were cultured under derepressing conditions for INO1 expression. However, the ß-galactosidase gene fused with the INO1 promoter region was expressed normally in the scs2{Delta} strain. The phospholipid composition of scs2{Delta} cells was not dramatically changed compared with wild-type cells at 28°C, but the phosphatidylinositol level was reduced in scs2{Delta} cells cultured at 34°C. In addition, elevated phosphatidylcholine synthesis through the CDP-choline pathway was observed in the scs2{Delta} strain, and the disruption of genes involved in the CDP-choline pathway rescued the INO1 expression defect of the scs2{Delta} strain. These results indicate that Scs2p can contribute to coordinated phospholipid metabolism including INO1 expression by regulating phosphatidylcholine synthesis through the CDP-choline pathway.

+ To whom correspondence should be addressed. Tel/Fax: +81-742-20-3420, E-mail: kagiwada{at}cc.nara-wu.ac.jp


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