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.

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