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The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating enzyme.

The N-end rule relates the in vivo half-life of a protein to the identity of its amino-terminal residue. Distinct versions of the N-end rule operate in all organisms examined, from mammals to bacteria. We show that UBC2(RAD6), one of at least seven ubiquitin-conjugating enzymes in the yeast Saccharomyces cerevisiae, is essential for multiubiquitination and degradation of the N-end rule substrates. We also show that UBC2 is physically associated with UBR1, the recognition component of the N-end rule pathway. These results indicate that some of the UBC2 functions, which include DNA repair, induced mutagenesis, sporulation, and regulation of retrotransposition, are mediated by protein degradation via the N-end rule pathway.

Pubmed ID: 1651502


  • Dohmen RJ
  • Madura K
  • Bartel B
  • Varshavsky A


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

August 15, 1991

Associated Grants

  • Agency: NIDDK NIH HHS, Id: DK39520
  • Agency: NIGMS NIH HHS, Id: GM31530

Mesh Terms

  • DNA Repair
  • Fungal Proteins
  • Haploidy
  • Ligases
  • Models, Biological
  • Protein Binding
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitins