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A more recent version of this article appeared on April 1, 2003
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Submitted on August 2, 2002
Revised on November 14, 2002
Accepted on December 4, 2002
1 Institut für Biochemie, Universität Stuttgart, Pfaffenwaldring 55, 70569 Stuttgart, Germany
2 Czech Academy of Sciences, Institute of Physiology, Videnska 1083, 14220 Prague, Czech Republic
3 Institut für Mikrobiologie, Johann Wolfgang Goethe-Universität Frankfurt, Marie-Curie-Straße 9, 60439 Frankfurt, Germany
* Corresponding author. E-mail address: dieter.wolf{at}po.uni-stuttgart.de.
Metabolic adaptation of Saccharomyces cerevisiae cells from a non-fermentable carbon source to glucose induces selective, rapid breakdown of the gluconeogenetic key enzyme fructose-1,6-bisphosphatase (FBPase), a process called catabolite degradation. Here we identify eight novel GID-genes, required for proteasome dependent catabolite degradation of FBPase. Four yeast proteins contain the CTLH domain of unknown function. All of them are Gid-proteins.
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