Ump1p Is Required for Proper Maturation of the 20S Proteasome and Becomes Its Substrate upon Completion of the Assembly

• Published in: Cell 1998-02, Vol.92 (4), p.489-499
• Main Authors: Ramos, Paula C, Höckendorff, Jörg, Johnson, Erica S, Varshavsky, Alexander, Dohmen, R.Jürgen
• Format: Article
• Language: English
• Subjects: Cysteine Endopeptidases; Endopeptidases - genetics; Fungal Proteins - genetics; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Fungal; Molecular Chaperones - genetics; Molecular Chaperones - metabolism; Molecular Sequence Data; Mutagenesis; Proteasome Endopeptidase Complex; Protein Precursors - metabolism; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae Proteins; Sequence Homology, Amino Acid; Spores, Fungal - physiology; Substrate Specificity; Ubiquitins - metabolism
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/S0092-8674(00)80942-3

We report the discovery of a short-lived chaperone that is required for the correct maturation of the eukaryotic 20S proteasome and is destroyed at a specific stage of the assembly process. The S. cerevisiae Ump1p protein is a component of proteasome precursor complexes containing unprocessed β subunits but is not detected in the mature 20S proteasome. Upon the association of two precursor complexes, Ump1p is encased and is rapidly degraded after the proteolytic sites in the interior of the nascent proteasome are activated. Cells lacking Ump1p exhibit a lack of coordination between the processing of β subunits and proteasome assembly, resulting in functionally impaired proteasomes. We also show that the propeptide of the Pre2p/Doa3p β subunit is required for Ump1p's function in proteasome maturation.