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Plant Physiol, November 2001, Vol. 127, pp. 792-802

Antisense Inhibition of Threonine Synthase Leads to High Methionine Content in Transgenic Potato Plants1

Michaela Zeh, Anna Paola Casazza,2 Oliver Kreft, Ute Roessner, Katrin Bieberich, Lothar Willmitzer, Rainer Hoefgen,* and Holger Hesse

Max-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476 Golm, Germany (M.Z., A.P.C., O.K., U.R., K.B., L.W., R.H.); and Freie Universität Berlin, Institut für Biologie, Angewandte Genetik, Albrecht-Thaer-Weg 6, 14195 Berlin, Germany (H.H.)

Methionine (Met) and threonine (Thr) are members of the aspartate family of amino acids. In plants, their biosynthetic pathways diverge at the level of O-phosphohomo-serine (Ser). The enzymes cystathionine gamma-synthase and Thr synthase (TS) compete for the common substrate O-phosphohomo-Ser with the notable feature that plant TS is activated through S-adenosyl-Met, a metabolite derived from Met. To investigate the regulation of this branch point, we engineered TS antisense potato (Solanum tuberosum cv Désirée) plants using the constitutive cauliflower mosaic virus 35S promoter. In leaf tissues, these transgenics exhibit a reduction of TS activity down to 6% of wild-type levels. Thr levels are reduced to 45% wild-type controls, whereas Met levels increase up to 239-fold depending on the transgenic line and environmental conditions. Increased levels of homo-Ser and homo-cysteine indicate increased carbon allocation into the aspartate pathway. In contrast to findings in Arabidopsis, increased Met content has no detectable effect on mRNA or protein levels or on the enzymatic activity of cystathionine gamma-synthase in potato. Tubers of TS antisense potato plants contain a Met level increased by a factor of 30 and no reduction in Thr. These plants offer a major biotechnological advance toward the development of crop plants with improved nutritional quality.


1 This project was partially supported by the European Framework Programme 4 (project grant no. Bio-4CT-97-2182) and by the Max-Planck-Society.

2 Present address: University of Milan, Plant Physiology and Biochemistry Section, Biology Department, Via Celoria 26, Milan 20133, Italy.

* Corresponding author; e-mail hoefgen{at}mpimp-golm.mpg.de; fax 49-331-5678201.

© 2001 American Society of Plant Physiologists



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