First published online February 24, 2002; 10.1104/pp.010887
Plant Physiol, March 2002, Vol. 128, pp. 1109-1119
-Glutamyl Transpeptidase in Transgenic Tobacco Plants.
Cellular Localization, Processing, and Biochemical
Properties1
Sergei
Storozhenko,
Enric
Belles-Boix,2
Elena
Babiychuk,
Didier
Hérouart,
Mark W.
Davey,3
Luit
Slooten,
Marc
Van Montagu,
Dirk
Inzé,* and
Sergei
Kushnir
Vakgroep Moleculaire Genetica, Departement Plantengenetica, Vlaams
Interuniversitair Instituut voor Biotechnologie, Universiteit Gent,
K.L. Ledeganckstraat 35, B-9000 Gent, Belgium (S.S., E.B.-B., E.B.,
M.W.D., M.V.M., D.I., S.K.); Laboratoire de Biologie
Végétale et Microbiologie, Université de Nice,
F-06108 Nice cedex 2, France (D.H.); and Laboratorium voor Biofysica,
Vrije Universiteit Brussel, B-1050 Brussels, Belgium (L.S.)
-Glutamyl transpeptidase ( -GT) is a ubiquitous enzyme
that catalyzes the first step of glutathione (GSH) degradation in the
-glutamyl cycle in mammals. A cDNA encoding an Arabidopsis homolog
for -GT was overexpressed in tobacco (Nicotiana
tabacum) plants. A high level of the membrane-bound -GT
activity was localized outside the cell in transgenic plants. The
overproduced enzyme was characterized by a high affinity to GSH and was
cleaved post-translationally in two unequal subunits. Thus, Arabidopsis
-GT is similar to the mammalian enzymes in enzymatic properties,
post-translational processing, and cellular localization, suggesting
analogous biological functions as a key enzyme in the catabolism of GSH.
1
This work was supported by the Fund for
Scientific Research Flanders (grant no. G004796).
2
Present address: Laboratoire de Biologie Cellulaire,
Institut National de la Recherche Agronomique, Route de St-Cyr,
F-78026 Versailles cedex, France.
3
Present address: Fruitteeltcentrum, Willem de Croylaan
442, B-3001 Heverlee, Belgium.
*
Corresponding author; e-mail diinz{at}gengenp.rug.ac.be; fax
32-9-264-5349.
© 2002 American Society of Plant Physiologists
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