In vivo function of the proteasome in the ubiquitin pathway. |
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Authors: | W Seufert and S Jentsch |
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Institution: | Friedrich-Miescher-Laboratorium der Max-Planck-Gesellschaft, Tübingen, Germany. |
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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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