Abstract：
: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 beta 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 beta subunits and proteasome assembly, resulting in functionally impaired proteasomes. We also show that the propeptide of the Pre2p/Doa3p beta subunit is required for Ump1p's function in proteasome maturation.
journal_name
Celljournal_title
Cellauthors
Ramos PC,Höckendorff J,Johnson ES,Varshavsky A,Dohmen RJdoi
10.1016/s0092-8674(00)80942-3subject
Has Abstractpub_date
1998-02-20 00:00:00pages
489-99issue
4eissn
0092-8674issn
1097-4172pii
S0092-8674(00)80942-3journal_volume
92pub_type
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