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

Cell | Mar 5, 1999

http://www.ncbi.nlm.nih.gov/pubmed/10089880

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 RIS Download

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

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Associated grants

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

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