Title: Expression of Escherichia coli otsA in a Saccharomyces cerevisiae tps1 mutant restores trehalose 6-phosphate levels and partly restores growth and fermentation with glucose and control of glucose influx into glycolysis
Authors: Bonini, BM
Van Vaeck, Christophe
Larsson, C
Gustafsson, L
Ma, PS
Winderickx, Joris
Van Dijck, Patrick
Thevelein, Johan # ×
Issue Date: Aug-2000
Publisher: Portland press
Series Title: Biochemical journal vol:350 pages:261-268
Abstract: The TPS1 gene, encoding trehalose-6-phosphate synthase (TPS), exerts an essential control on the influx of glucose into glycolysis in the yeast Saccharomyces cerevisiae. The deletion of TPS1 causes an inability to grow on glucose because of a hyperaccumulation of sugar phosphates and depletion of ATP and phosphate, We show that expression of the Escherichia coli homologue, otsA, in a yeast tpsl mutant results in high TPS activity. Although the trehalose 6-phosphate (Tre6P) level durning exponential growth on glucose was at least as high as in a wildtype yeast strain, growth on glucose was only partly restored and the lag phase was much longer. Measurement of the glycolytic metabolites immediately after the addition of glucose showed that in spite of a normal Tre6P accumulation there was still a partial hyperaccumulation of sugar phosphates. Strong elevation of the Tre6P level by the additional deletion of the TPS2 gene, which encodes Tre6P phosphatase, was not able to cause a strong decrease in the sugar phosphate levels in comparison with the wild-type strain. In addition, in chemostat experiments the short-term response to a glucose pulse was delayed, but normal metabolism was regained over a longer period. These results show that Tre6P synthesis from a heterologous TPS enzyme can to some extent restore the control of glucose influx into glycolysis and growth on glucose in yeast. However, they also indicate that the yeast TPS enzyme, as opposed to the E. coli otsA gene product, is able to increase the efficiency of the Tre6P control on glucose influx into yeast glycolysis.
ISSN: 0264-6021
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Physiology of Plants and Micro-organisms Section - miscellaneous
Molecular Microbiology and Biotechnology Section - miscellaneous
× corresponding author
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science