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Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53.

The E6 protein of the oncogenic human papillomavirus types 16 and 18 facilitates the rapid degradation of the tumor-suppressor protein p53 via the ubiquitin-dependent proteolytic pathway. The E6 protein binds to a cellular protein of 100 kDa termed E6-AP. The complex of E6 and E6-AP specifically interacts with p53 and induces the ubiquitination of p53 in a reaction which requires the ubiquitin-activating enzyme (E1) and a cellular fraction thought to contain a mammalian ubiquitin-conjugating enzyme (E2). This mammalian E2 activity could be replaced with bacterially expressed UBC8 from Arabidopsis thaliana, which belongs to a subfamily of E2s including yeast UBC4 and UBC5 which are highly conserved at the amino acid level. In this paper we describe the cloning of a human cDNA encoding a human E2 that we have designated UbcH5 and that is related to Arabidopsis UBC8 and the other members of this subfamily. We demonstrate that UbcH5 can function in the E6/E6-AP-induced ubiquitination of p53.

Pubmed ID: 8090726

Authors

  • Scheffner M
  • Huibregtse JM
  • Howley PM

Journal

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

Publication Data

September 13, 1994

Associated Grants

None

Mesh Terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary
  • Ligases
  • Molecular Sequence Data
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Tumor Suppressor Protein p53
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligases
  • Ubiquitins
  • Viral Proteins