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Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair.

Ubiquitin-conjugating enzyme variant (UEV) proteins resemble ubiquitin-conjugating enzymes (E2s) but lack the defining E2 active-site residue. The MMS2-encoded UEV protein has been genetically implicated in error-free postreplicative DNA repair in Saccharomyces cerevisiae. We show that Mms2p forms a specific heteromeric complex with the UBC13-encoded E2 and is required for the Ubc13p-dependent assembly of polyubiquitin chains linked through lysine 63. A ubc13 yeast strain is UV sensitive, and single, double, and triple mutants of the UBC13, MMS2, and ubiquitin (ubiK63R) genes display a comparable phenotype. These findings support a model in which an Mms2p/Ubc13p complex assembles novel polyubiquitin chains for signaling in DNA repair, and they suggest that UEV proteins may act to increase diversity and selectivity in ubiquitin conjugation.

Pubmed ID: 10089880


  • Hofmann RM
  • Pickart CM



Publication Data

March 5, 1999

Associated Grants

  • Agency: NIDDK NIH HHS, Id: DK46984
  • Agency: NIEHS NIH HHS, Id: T32 ES07141

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Biopolymers
  • Cattle
  • DNA Repair
  • Fungal Proteins
  • Humans
  • Ligases
  • Macromolecular Substances
  • Molecular Sequence Data
  • Multigene Family
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Species Specificity
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligases
  • Ubiquitins