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Plant and Cell Physiology, 2000, Vol. 41, No. 9 1080-1084
© 2000 Oxford University Press

cDNA Cloning and Expression of an Aminoalcoholphosphotransferase Isoform in Chinese Cabbage

Young Hee Choi1, Jin Kyung Lee1, Choon-Hwan Lee2 and Sung Ho Cho 1,3

1 Department of Biology, Inha University, Inchon 402-751, Korea 2 Department of Molecular Biology, Pusan National University, Pusan 609-735, Korea

Aminoalcoholphosphotransferase (AAPT) catalyzes the synthesis of phosphatidylcholine and phosphatidylethanolamine from diacylglycerol plus a CDP-aminoalcohol such as CDP-choline or CDP-ethanolamine. Previously we reported the cloning of a cDNA encoding this enzyme from Chinese cabbage roots, and suggested the presence of possible isoforms [Min et al. (1997) J. Plant Biol. 40: 234]. We now report the cDNA cloning and expression analysis of a second AAPT from Chinese cabbage. This AAPT cDNA, AAPT2, contains an open reading frame of 1,170 bp coding for a protein of 389 amino acids. It shares 95% identity and 96% similarity with Chinese cabbage AAPT1 at the deduced amino acid level. The results from reverse transcriptase-PCR indicate that expression of AAPT2 is regulated temporally and up-regulated by low temperature.

3 Corresponding author: E-mail, shcho@inha.ac.kr; Fax, +82-32-874-6737.


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