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J. Biol. Chem., Vol. 282, Issue 47, 34288-34298, November 23, 2007

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LPT1 Encodes a Membrane-bound O-Acyltransferase Involved in the Acylation of Lysophospholipids in the Yeast Saccharomyces cerevisiae^*

Hisanori Tamaki¹, Atsushi Shimada, Yoshihiro Ito, Mihoko Ohya, Juri Takase, Masahiro Miyashita^¶, Hisashi Miyagawa^¶, Hiroyuki Nozaki, Reiko Nakayama^||, and Hidehiko Kumagai^**

From the Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, the Division of Integrated Life Science, Graduate School of Biostudies, and ^¶Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, the ^||Department of Food Science, Kyoto Women's University, Kyoto 606, and the ^**Research Institute of Bioresources and Biotechnology, Ishikawa Prefectural University, Ishikawa 921-8836, Japan

Phospholipids are major components of cellular membranes that participate in a range of cellular processes. Phosphatidic acid (PA) is a key molecule in the phospholipid biosynthetic pathway. In Saccharomyces cerevisiae, SLC1 has been identified as the gene encoding lysophosphatidic acid acyltransferase, which catalyzes PA synthesis. However, despite the importance of PA, disruption of SLC1 does not affect cell viability (Nagiec, M. M., Wells, G. B., Lester, R. L., and Dickson, R. C. (1993) J. Biol. Chem. 268, 22156–22163). We originally aimed to identify the acetyl-CoA:lyso platelet-activating factor acetyltransferase (lysoPAF AT) gene in yeast. Screening of a complete set of yeast deletion clones (4741 homozygous diploid clones) revealed a single mutant strain, YOR175c, with a defect in lysoPAF AT activity. YOR175c has been predicted to be a member of the membrane-bound O-acyltransferase superfamily, and we designated the gene LPT1. An Lpt1-green fluorescent protein fusion protein localized at the endoplasmic reticulum. Other than lysoPAF AT activity, Lpt1 catalyzed acyltransferase activity with a wide variety of lysophospholipids as acceptors, including lysophosphatidic acid, lysophosphatidylcholine, lysophosphatidylethanolamine, lysophosphatidylglycerol, lysophosphatidylinositol, and lysophosphatidylserine. A liquid chromatography-mass spectrometry analysis indicated that lysophosphatidylcholine and lysophosphatidylethanolamine accumulated in the lpt1 mutant strain. Although the lpt1 mutant strain did not show other detectable defects, the lpt1 slc1 double mutant strain had a synthetic lethal phenotype. These results indicate that, in concert with Slc1, Lpt1 plays a central role in PA biosynthesis, which is essential for cell viability.

Received for publication, June 1, 2007 , and in revised form, September 21, 2007.

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBank^TM/EBI Data Bank with accession number(s) AB305041 [GenBank] , AB305042 [GenBank] , AB305043 [GenBank] , AB305044 [GenBank] , AB305045 [GenBank] , AB305046 [GenBank] , AB305047 [GenBank] , and AB305048 [GenBank] .

^* This work was supported in part by Grants-in-Aid from the Ministry of Education, Science, Culture, Sports, and Technology of Japan (to H. T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2.

¹ To whom correspondence should be addressed. Tel./Fax: 81-99-285-3543; E-mail: noritama{at}ms.kagoshima-u.ac.jp.

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