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Cloning and functional characterization of 2-C-methyl-d-erythritol 4-phosphate cytidyltransferase (GbMECT) gene from Ginkgo biloba.

Kim SM, Kuzuyama T, Chang YJ, Kwon HJ, Kim SU

Program in Applied Life Chemistry, School of Agricultural Biotechnology, Seoul National University, Sinlim-dong, Gwanak-gu, Seoul 151-921, Republic of Korea; Plant Metabolism Research Center, Kyung Hee University, Yongin 449-701, Republic of Korea.

2-C-methyl-d-erythritol 4-phosphate cytidyltransferase (MECT), the third enzyme of the 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway, catalyzes formation of 4-(cytidine 5'-diphospho)-2-C-methyl-d-erythritol from MEP. GbMECT, presumably involved in ginkgolide biosynthesis, was cloned and characterized from Ginkgo biloba embryonic roots. The protein containing the N-terminal chloroplast transit peptide consisted of 327 amino acid residues. Complementation of GbMECT with Escherichia coli NMW33, ygbP (EcMECT) knock-out mutant, rescued the mutant, confirming the function of the protein. Transcription levels of GbMECT remained generally constant in embryonic roots and leaves for 1month. Full 88 N-terminal residues were necessary to deliver the protein into the chloroplast as shown by protein-targeting analysis with GFP as a reporter protein in Arabidopsis thaliana protoplasts.

Published 28 July 2006 in Phytochemistry, 67(14): 1435-41.
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