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Originally published In Press as doi:10.1074/jbc.R400032200 on December 6, 2004
J. Biol. Chem., Vol. 280, Issue 4, 2397-2400, January 28, 2005
Minireview
Three Enzyme Systems for Galactoglycerolipid Biosynthesis Are Coordinately Regulated in Plants*
Christoph Benning and
Hiroyuki Ohta¶
From the
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824-1319 and the ¶Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan
Galactoglycerolipids, in which galactose is bound at the glycerol sn-3 position in O-glycosidic linkage to diacylglycerol, are abundant in plants and photosynthetic bacteria, where they constitute the bulk of the polar lipids of the photosynthetic membranes. Galactoglycerolipid biosynthesis in plants is highly compartmentalized involving enzymes at the endoplasmic reticulum and the two chloroplast envelopes. This peculiar organization requires extensive trafficking of lipid precursors. It is now increasingly apparent that there are three different sets of lipid galactosyltransferases capable of galactoglycerolipid biosynthesis in the model plant Arabidopsis. Two enzymes, MGD1 and DGD1, provide the bulk of galactoglycerolipids in the chloroplast and in photosynthetic tissues in general. Under phosphate-limited growth conditions and in non-photosynthetic tissues MGD2/3 and DGD2 are highly active. Moreover, galactoglycerolipids produced by this second pathway are often found in extraplastidic membranes. Although these galactosyltransferases use UDP-Gal as the galactose donor, a third pathway involves a processive enzyme, which transfers galactose from one galactolipid to another.
* This minireview will be reprinted in the 2005 Minireview Compendium, which will be available in January, 2006. Work in the laboratory of C. B. is funded by grants from the Department of Energy, the National Science Foundation, the Department of Agriculture, and BASF Plant Science. Work in the laboratory of H. O. is funded by Grant-in-Aid for Scientific Research on Priority Areas 15380049 from the Ministry of Education, Sports, Science and Culture in Japan.
To whom correspondence should be addressed. Tel.: 517-355-1609; Fax: 517-353-9334; E-mail: benning{at}msu.edu.

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