cDNA Cloning and Expression of an Aminoalcoholphosphotransferase Isoform in Chinese Cabbage | Zendy

Young Hee Choi | Zendy; Jin Kyung Lee | Zendy; Choon-Hwan Lee | Zendy; Sung Ho Cho | Zendy

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cDNA Cloning and Expression of an Aminoalcoholphosphotransferase Isoform in Chinese Cabbage

Author(s) -

Young Hee Choi,

Jin Kyung Lee,

Choon-Hwan Lee,

Sung Ho Cho

Publication year - 2000

Publication title -

plant and cell physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.975

H-Index - 152

eISSN - 1471-9053

pISSN - 0032-0781

DOI - 10.1093/pcp/pcd030

Subject(s) - complementary dna , open reading frame , cloning (programming) , microbiology and biotechnology , amino acid , gene isoform , biology , biochemistry , molecular cloning , diacylglycerol kinase , cdna library , chemistry , enzyme , peptide sequence , gene , protein kinase c , computer science , programming language

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.

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