Plant Physiol.
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Plant Physiology 93:1286-1294 (1990)
© 1990 American Society of Plant Biologists

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Metabolism and Enzymology

Biosynthesis of Digalactosyldiacylglycerol in Plastids from 16:3 and 18:3 Plants 1

Johan W. M. Heemskerk2, Thomas Storz3, Richard R. Schmidt3 and Ernst Heinz

Institut für Allgemeine Botanik, University of Hamburg, Ohnhorststr. 18, 2000 Hamburg 52, Federal Republic of Germany

Intact chloroplasts isolated from leaves of eight species of 16:3 and 18:3 plants and chromoplasts isolated from Narcissus pseudonarcissus L. flowers synthesize galactose-labeled mono-, di-, and trigalactosyldiacylglycerol (MGDG, DGDG, and TGDG) when incubated with UDP-[6-3H]galactose. In all plastids, galactolipid synthesis, and especially synthesis of DGDG and TGDG, is reduced by treatment of the organelles with the nonpenetrating protease thermolysin. Envelope membranes isolated from thermolysin-treated chloroplasts of Spinacia oleracea L. (16:3 plant) and Pisum sativum L. (18:3 plant) or membranes isolated from thermolysin-treated chromoplasts are strongly reduced in galactolipid:galactolipid galactosyltransferase activity, but not with regard to UDP-Gal:diacylglycerol galactosyltransferase. For the intact plastids, this indicates that thermolysin treatment specifically blocks DGDG (and TGDG) synthesis, whereas MGDG synthesis is not affected. Neither in chloroplast nor in chromoplast membranes is DGDG synthesis stimulated by UDP-Gal. DGDG synthesis in S. oleracea chloroplasts is not stimulated by nucleoside 5'-diphospho digalactosides. Therefore, galactolipid:galactolipid galactosyltransferase is so far the only detectable enzyme synthesizing DGDG. These results conclusively suggest that the latter enzyme is located in the outer envelope membrane of different types of plastids and has a general function in DGDG synthesis, both in 16:3 and 18:3 plants.

2 Present address and corresponding address: Department of Biochemistry, B.M.C., University of Limburg, P.O. 616, 6200 MD Maastricht, The Netherlands.

3 Faculty of Chemistry, University of Konstanz, Konstanz, Federal Republic of Germany.

1 This paper is dedicated to Jef F. G. M. Wintermans, Nijmegen (The Netherlands) on the occasion of his 68th birthday in 1989. The investigations were supported by the Deutsche Forschungsgemeinschaft. J. H. received a grant from the Federation of European Biochemical Societies.




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