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Plant Cell, Vol. 10, 1759-1768, October 1998, Copyright © 1998, American Society of Plant Physiologists

Targeting of Active Sialyltransferase to the Plant Golgi Apparatus

Edmund G.-T. Weea, D. Janine Sherriera, Tracy A. Primea, and Paul Dupreea
a Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, United Kingdom

Correspondence to: Paul Dupree, P.Dupree{at}bioc.cam.ac.uk (E-mail), 44-1223-333345 (fax).

Glycosyltransferases in the Golgi apparatus synthesize cell wall polysaccharides and elaborate the complex glycans of glycoproteins. To investigate the targeting of this type of enzyme to plant Golgi compartments, we generated transgenic Arabidopsis plants expressing {alpha}-2,6-sialyltransferase, a glycosyltransferase of the mammalian trans-Golgi cisternae and the trans-Golgi network. Biochemical analysis as well as immunolight and immunoelectron microscopy of these plants indicate that the protein is targeted specifically to the Golgi apparatus. Moreover, the protein is predominantly localized to the cisternae and membranes of the trans side of the organelle. When supplied with the appropriate substrates, the enzyme has significant {alpha}-2,6-sialyltransferase activity. These results indicate a conservation of glycosyltransferase targeting mechanisms between plant and mammalian cells and also demonstrate that glycosyltransferases can be subcompartmentalized to specific cisternae of the plant Golgi apparatus.




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