Ubiquitin, a central component of selective cytoplasmic proteolysis, is linked to proteins residing at the locus of non-selective proteolysis, the vacuole.
Ubiquitin, an evolutionary highly conserved protein, is known to be involved in selective proteolysis 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.
Simeon
A
A
Institut für Biochemie, Universität Stuttgart, Germany.
van der Klei
I J
IJ
Veenhuis
M
M
Wolf
D H
DH
D016282:Aspartic Acid Endopeptidases / Q000235:genetics / Q000378:metabolism; D003593:Cytoplasm / Q000201:enzymology; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D015151:Immunoblotting; D008854:Microscopy, Electron; D009154:Mutation; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism; D014452:Ubiquitins / Q000378:metabolism*; D014617:Vacuoles / Q000378:metabolism*
D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; D014452:Ubiquitins; D012697:Serine Endopeptidases; C023302:yeast proteinase B; C022325:aspartic proteinase A; C499267:PEP4 protein, S cerevisiae; D016282:Aspartic Acid Endopeptidases