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J Biol Chem, Vol. 273, Issue 31, 19443-19452, July 31, 1998

Mutations in the Yeast Proteasome -Type Subunit Pre3 Uncover Position-dependent Effects on Proteasomal Peptidase Activity and in Vivo Function

Roland Gueckel, Cordula Enenkel^§, Dieter H. Wolf, and Wolfgang Hilt

From the  Institut für Biochemie, Universität Stuttgart, Pfaffenwaldring 55, 70569 Stuttgart and the ^§ Institut für Biochemie, Charité der Humboldt Universität zu Berlin, Monbijoustrasse 2A, 10117 Berlin, Germany

Proteasomes are highly complex proteases responsible for selective protein degradation in the eukaryotic cell. 26 S proteasomes consist of two regulatory 19 S cap complexes and the 20 S proteasome, which acts as the proteolytic core module. We isolated six mutants of the yeast Saccharomyces cerevisiae containing mutations in the 20 S proteasome -type subunit Pre3. Three mutations (pre3-2, pre3-3, and pre3-5) which reside at the active site cleft of the Pre3 subunit solely caused reduction of the proteasomal peptidylglutamyl peptide-hydrolyzing activity but did not lead to detectable defects in protein degradation nor to any other phenotype. However, the pre3-2 mutation strengthened phenotypes induced by other 20 S proteasomal mutations, indicating that the peptidylglutamyl peptide-hydrolyzing activity has to fulfill some rescue functions. The other three mutations (pre3-1, pre3-4, and pre3-6) are located at diverse sites of the Pre3 protein and caused multiple defects in proteasomal peptide cleaving activities. pre3-1 and pre3-6 mutants exhibited significant defects in proteasomal protein degradation; they accumulated ubiquitinated proteins and stabilized defined substrate proteins as, e.g. fructose-1,6-bisphosphatase. In addition, pre3-1 and pre3-6 mutant cells exhibited pleiotropic phenotypes as temperature sensitivity and cell cycle-related effects.

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