Ubiquitin, a central component of selective cytoplasmic proteolysis, is linked to proteins residing at the locus of non-selective proteolysis, the vacuole

A Simeon; I J van der Klei; M Veenhuis; D H Wolf

doi:10.1016/0014-5793(92)81254-j

Ubiquitin, a central component of selective cytoplasmic proteolysis, is linked to proteins residing at the locus of non-selective proteolysis, the vacuole

FEBS Lett. 1992 Apr 20;301(2):231-5. doi: 10.1016/0014-5793(92)81254-j.

Authors

A Simeon¹, I J van der Klei, M Veenhuis, D H Wolf

Affiliation

¹ Institut für Biochemie, Universität Stuttgart, Germany.

PMID: 1314742
DOI: 10.1016/0014-5793(92)81254-j

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Aspartic Acid Endopeptidases / genetics
Aspartic Acid Endopeptidases / metabolism
Cytoplasm / enzymology
Fungal Proteins / genetics
Fungal Proteins / metabolism*
Immunoblotting
Microscopy, Electron
Mutation
Saccharomyces cerevisiae / genetics
Saccharomyces cerevisiae / metabolism*
Saccharomyces cerevisiae / ultrastructure
Saccharomyces cerevisiae Proteins
Serine Endopeptidases / genetics
Serine Endopeptidases / metabolism
Ubiquitins / metabolism*
Vacuoles / metabolism*

Substances

Fungal Proteins
Saccharomyces cerevisiae Proteins
Ubiquitins
Serine Endopeptidases
yeast proteinase B
aspartic proteinase A
PEP4 protein, S cerevisiae
Aspartic Acid Endopeptidases