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Updated: Aug 11, 2026

Assaying Proteasomal Degradation in a Cell-free System in Plants
Published on: March 26, 2014
In vivo function of the proteasome in the ubiquitin pathway
1Friedrich-Miescher-Laboratorium der Max-Planck-Gesellschaft, Tübingen, Germany.
Abstract:
A major eukaryotic proteolytic system is known to require the covalent attachment of ubiquitin to substrates prior to their degradation, yet the proteinase involved remains poorly defined. The proteasome, a large conserved multi-subunit protein complex of the cytosol and the nucleus, has been implicated in a variety of cellular functions. It is shown here that a yeast mutant with a defective proteasome fails to degrade proteins which are subject to ubiquitin-dependent proteolysis in wild-type cells. Thus, the proteasome is part of the ubiquitin system and mediates the degradation of ubiquitin-protein conjugates in vivo.
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