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Vol. 14, Issue 4, 1652-1663, April 2003

Catabolite Degradation of Fructose-1,6-bisphosphatase in the Yeast Saccharomyces cerevisiae: A Genome-wide Screen Identifies Eight Novel GID Genes and Indicates the Existence of Two Degradation Pathways

Jochen Regelmann,^* Thomas Schüle,^* Frank S. Josupeit,^* Jaroslav Horak, Matthias Rose,^§ Karl-Dieter Entian,^§ Michael Thumm, and Dieter H. Wolf

 Institut für Biochemie, Universität Stuttgart, 70569 Stuttgart, Germany;  Czech Academy of Sciences, Institute of Physiology, 14220 Prague, Czech Republic; and  ^§Institut für Mikrobiologie, Johann Wolfgang Goethe-Universität Frankfurt, 60439 Frankfurt, Germany

Metabolic adaptation of Saccharomyces cerevisiae cells from a nonfermentable carbon source to glucose induces selective, rapid breakdown of the gluconeogenetic key enzyme fructose-1,6-bisphosphatase (FBPase), a process called catabolite degradation. Herein, 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. The site of catabolite degradation has been controversial until now. Two FBPase degradation pathways have been described, one dependent on the cytosolic ubiquitin-proteasome machinery, and the other dependent on vacuolar proteolysis. Interestingly, three of the novel Gid proteins involved in ubiquitin-proteasome-dependent degradation have also been reported by others to affect the vacuolar degradation pathway. As shown herein, additional genes suggested to be essential for vacuolar degradation are unnecessary for proteasome-dependent degradation. These data raise the question as to whether two FBPase degradation pathways exist that share components. Detailed characterization of Gid2p demonstrates that it is part of a soluble, cytosolic protein complex of at least 600 kDa. Gid2p is necessary for FBPase ubiquitination. Our studies have not revealed any involvement of vesicular intermediates in proteasome-dependent FBPase degradation. The influence of Ubp14p, a deubiquitinating enzyme, on proteasome-dependent catabolite degradation was further uncovered.

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^* These authors contributed equally to this work.

Corresponding author. E-mail address: dieter.wolf{at}po.uni-stuttgart.de.

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Molecular Biology of the Cell
Vol. 14, 1652-1663, April 2003
Copyright © 2003 by The American Society for Cell Biology

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