In vivo function of the proteasome in the ubiquitin pathway

Seufert, W; Jentsch, S

doi:10.1002/j.1460-2075.1992.tb05379.x

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In vivo function of the proteasome in the ubiquitin pathway

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Seufert, W
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Jentsch, S
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Seufert, W., & Jentsch, S. (1992). In vivo function of the proteasome in the ubiquitin pathway. EMBO Journal, 11(8), 3077-3080. doi:10.1002/j.1460-2075.1992.tb05379.x.

Cite as: https://hdl.handle.net/21.11116/0000-000B-F6E3-F

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.