Plant Physiology Preview
Published on April 9, 2002; 10.1104/pp.010948
Received October 15, 2001
Returned for revision November 23, 2001
Accepted January 30, 2002
Direct Interference with Rhamnogalacturonan I Biosynthesis in
Golgi Vesicles
Michael Skjøt , Markus Pauly , Maxwell S. Bush , Bernhard Borkhardt , Maureen C. McCann , and Peter Ulvskov *
Biotechnology Group, Danish Institute of Agricultural Sciences, Thorvaldsensvej 40, 1871 Copenhagen, Denmark (M.S., B.B., P.U.); Department of Plant Biology, Plant Biochemistry Laboratory, The Royal Veterinary and Agricultural University, Thorvaldsensvej 40, 1871 Copenhagen, Denmark (M.P.); and Department of Cell and Developmental Biology, John Innes Centre, Norwich Research Park, Colney Lane, NR4 7UH Norwich, United Kingdom (M.S.B., M.C.M.)
* Corresponding author; email: p.ulvskov{at}dias.kvl.dk.
Pectin is a class of complex cell wall polysaccharides with multiple roles during cell development. Assigning specific functions to particular polysaccharides is in its infancy, in part, because of the limited number of mutants and transformants available with modified pectic polymers in their walls. Pectins are also important polymers with diverse applications in the food and pharmaceutical industries, which would benefit from technology for producing pectins with specific functional properties. In this report, we describe the generation of potato (Solanum tuberosum L. cv Posmo) tuber transformants producing pectic rhamnogalacturonan I (RGI) with a low level of arabinosylation. This was achieved by the expression of a Golgi-membrane anchored endo- -1,5-arabinanase. Sugar composition analysis of RGI isolated from transformed and wild-type tubers showed that the arabinose content was decreased by approximately 70% in transformed cell walls compared with wild type. The modification of the RGI was confirmed by immunolabeling with an antibody recognizing -1,5-arabinan. This is the first time that the biosynthesis of a plant cell wall polysaccharide has been manipulated through the action of a glycosyl hydrolase targeted to the Golgi compartment.
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