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