Ubiquitin-mediated proteolysis of a short-lived regulatory protein depends on its cellular localization

J Biol Chem. 2000 Dec 15;275(50):39403-10. doi: 10.1074/jbc.M006949200.

Abstract

In this study we demonstrate that the Deg1 degradation signal of the transcriptional repressor Matalpha2 confers compartment-specific turnover to a reporter protein. Rapid degradation of a Deg1-containing fusion protein is observed only when the reporter is efficiently imported into the nucleus. In contrast, a reporter that is constantly exported from the nucleus exhibits an extended half-life. Furthermore, nuclear import functions are crucial for both Deg1-induced degradation as well as for the turnover of the endogenous Matalpha2 protein. The conjugation of ubiquitin to a Deg1-containing reporter protein is abrogated in mutants affected in nuclear import. Obviously, the Deg1 signal initiates rapid proteolysis within the nucleoplasm, whereas in the cytosol it mediates turnover via a slower pathway. In both pathways the ubiquitin-conjugating enzymes Ubc6p/Ubc7p play a pivotal role. These observations imply that both the cellular targeting of a substrate and the compartment-specific activity of components of the ubiquitin-proteasome system define the half-life of naturally short-lived proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / metabolism
  • Cell Nucleus / metabolism*
  • Cytoplasm / metabolism
  • Escherichia coli / metabolism
  • Fungal Proteins / metabolism*
  • Genes, Reporter
  • Green Fluorescent Proteins
  • Homeodomain Proteins / metabolism*
  • Intramolecular Transferases
  • Kinetics
  • Ligases / metabolism
  • Luminescent Proteins / metabolism
  • Membrane Proteins / metabolism
  • Microscopy, Fluorescence
  • Mutation
  • Plasmids / metabolism
  • Precipitin Tests
  • Protein Transport
  • Recombinant Fusion Proteins / metabolism
  • Repressor Proteins / metabolism*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Time Factors
  • Transcription, Genetic
  • Ubiquitin-Conjugating Enzymes*
  • Ubiquitins / metabolism*

Substances

  • CUE1 protein, S cerevisiae
  • Carrier Proteins
  • Fungal Proteins
  • Homeodomain Proteins
  • Luminescent Proteins
  • MATA2 protein, S cerevisiae
  • Membrane Proteins
  • Recombinant Fusion Proteins
  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins
  • Ubiquitins
  • Green Fluorescent Proteins
  • UBC6 protein, S cerevisiae
  • UBE2J1 protein, human
  • UBE2L3 protein, human
  • Ubiquitin-Conjugating Enzymes
  • Intramolecular Transferases
  • DEG1 protein, S cerevisiae
  • Ligases