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

http://www.ncbi.nlm.nih.gov/pubmed/8090726

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 RIS Download

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

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