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-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast Saccharomyces cerevisiaeLaboratoire de Physiologie et Ecologie Microbiennes, Section Interfacultaire d'Agronomie, Université Libre de Bruxelles c/o Institut Pasteur, Rue Engeland 642, B-1180, Brussels, Belgium
Author for correspondence: Michel J. Penninckx. Tel: +32 2 3733303. Fax: +32 2 3733174. e-mail: upemulb@resulb.ulb.ac.be
ABSTRACT
When the yeast Saccharomyces cerevisiae
1278b was starved for nitrogen, the total glutathione (GSH) pool increased from 7 to 17 nmol (mg dry wt)-1 during the first 2 h and then declined. More than 90% of the total GSH shifted towards the central vacuole during this time. This transient stimulation was not observed in the presence of buthionine-(S,R)-sulphoximine (BSO), a specific transition-state-analogue inhibitor of
-glutamylcysteine synthase (
-GCS), nor in a mutant strain deficient in this enzyme.
-Glutamyltranspeptidase (
-GT), a vacuolar enzyme responsible for the initial step of GSH degradation, was derepressed during nitrogen starvation. This mechanism can apparently enable the starved yeast cell to use the constituent amino acids from GSH which accumulate in the vacuole to satisfy its growth requirements for nitrogen.
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