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Published on May 19, 2006; 10.1104/pp.106.082859


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Received May 3, 2006
Returned for revision May 8, 2006
Accepted May 9, 2006

Comparative genomic analysis revealed a gene for monoglucosyldiacylglycerol synthase, an enzyme for photosynthetic membrane lipid synthesis in cyanobacteria

Koichiro Awai *, Takatoshi Kakimoto , Chie Awai , Takakazu Kaneko , Yuki Nakamura , Ken-ichiro Takamiya , Hajime Wada , and Hiroyuki Ohta

Graduate School for Bioscience and Biotechnology, Tokyo Institute of Technology, 4259-B-14 Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Japan
Kazusa DNA Research Institute, Kisarazu, Chiba, 292-0818, Japan
Graduate School for Bioscience and Biotechnology, Tokyo Institute of Technology, 4259-B-14 Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Japan; Research Center for the Evolving Earth and Planets, Tokyo Institute of Technology, 4259-B-14 Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Japan
Graduate School of Arts and Sciences, The University of Tokyo, Komaba, Tokyo, 153-8902, Japan

* Corresponding author; email: awai{at}molbiol.saitama-u.ac.jp.

Cyanobacteria have a thylakoid lipid composition very similar to that of plant chloroplasts, yet cyanobacteria are proposed to synthesize monogalactosyldiacylglycerol (MGDG), a major membrane polar lipid in photosynthetic membranes, by a different pathway. In addition, plant MGDG synthase has been cloned but no ortholog has been reported in cyanobacterial genomes. We report here the identification of the gene for monoglucosyldiacylglycerol (MGlcDG) synthase, which catalyzes the first step of galactolipid synthesis in cyanobacteria. Using comparative genomic analysis, candidates for the gene were selected based on the criteria that the enzyme activity is conserved between two species of cyanobacteria (unicellular (Synechocystis PCC6803) and filamentous (Anabaena PCC7120)) and we assumed three characteristics of the enzyme, namely that it harbors a glycosyltransferase motif, falls into a category of genes with unknown function and shares significant similarity in amino acid sequence between these two cyanobacteria. By motif search of all genes of Synechocystis, BLAST searches, and similarity searches between these two cyanobacteria, we identified four candidates for the enzyme which have all characteristics we predicted. When expressed in Escherichia coli, one of the Synechocystis candidate proteins showed MGlcDG synthase activity in a UDP-Glc dependent manner. The ortholog in Anabaena also showed the same activity. The enzyme was predicted to require a divalent cation for its activity and this was confirmed by biochemical analysis. The MGlcDG synthase and the plant MGDG synthase shared low similarity, supporting the presumption that cyanobacteria and plants utilize different pathway to synthesize MGDG.




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