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In vivo function of the proteasome in the ubiquitin pathway.
Author(s) -
Seufert W.,
Jentsch S.
Publication year - 1992
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1992.tb05379.x
Subject(s) - proteasome , ubiquitin , biology , proteolysis , protein degradation , microbiology and biotechnology , f box protein , genetics , ubiquitin ligase , biochemistry , enzyme , gene
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.