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Ubiquitin, a central component of selective cytoplasmic proteolysis, is linked to proteins residing at the locus of non‐selective proteolysis, the vacuole
Author(s) -
Simeon Angela,
van der Klei Ida J.,
Veenhuis Marten,
Wolf Dieter H.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81254-j
Subject(s) - proteolysis , vacuole , ubiquitin , cytoplasm , ubiquitins , microbiology and biotechnology , biology , organelle , biochemistry , ubiquitin ligase , chemistry , gene , enzyme
Ubiquitin, an evolutionary highly conserved protein, is known to be involved in selective protoolysis in the cytoplasm. Here we show that ubiquitin‐protein conjugates are also found in the yeast vacuole. Mutants defective in the major vacuolar endopeptidases, proteinase yscA and yscB, lead to accumulation of ubiquitin‐protein conjugates in this cellular organelle.