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Volume 272, Number 14, Issue of April 4, 1997 pp. 9567-9572
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Cloning of a Human cDNA for CTP-Phosphoethanolamine Cytidylyltransferase by Complementation in Vivo of a Yeast Mutant

(Received for publication, January 21, 1997)

Asae Nakashima , Kohei Hosaka ^§ and Jun-ichi Nikawa

From the  Department of Biochemical Engineering and Science, Faculty of Computer Science and Systems Engineering, Kyushu Institute of Technology, Iizuka, Fukuoka 820 and the ^§ Department of Biochemistry, Gunma University School of Medicine, Maebashi, Gunma 371, Japan

CTP-phosphoethanolamine cytidylyltransferase (ET) is the enzyme that catalyzes the formation of CDP-ethanolamine in the phosphatidylethanolamine biosynthetic pathway from ethanolamine. We constructed a Saccharomyces cerevisiae mutant of which the ECT1 gene, putatively encoding ET, was disrupted. This mutant showed a growth defect on ethanolamine-containing medium and a decrease of ET activity. A cDNA clone was isolated from a human glioblastoma cDNA expression library by complementation of the yeast mutant. Introduction of this cDNA into the yeast mutant clearly restored the formation of CDP-ethanolamine and phosphatidylethanolamine in cells. ET activity in transformants was higher than that in wild-type cells. The deduced protein sequence exhibited homology with the yeast, rat, and human CTP-phosphocholine cytidylyltransferases, as well as yeast ET. The cDNA gene product was expressed as a fusion with glutathione S-transferase in Escherichia coli and shown to have ET activity. These results clearly indicate that the cDNA obtained here encodes human ET.

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