Abstract
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.
Keywords
UbiquitinUbiquitin-conjugating enzymeUbiquitin ligaseBiologyArabidopsisUbiquitinsSubfamilyBiochemistryArabidopsis thalianaUbiquitin-Protein LigasesComplementary DNAEnzymeCell biologyMutantGene
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Publication Info
- Year
- 1994
- Type
- article
- Volume
- 91
- Issue
- 19
- Pages
- 8797-8801
- Citations
- 259
- Access
- Closed
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Cite This
Martin Scheffner,
Jon M. Huibregtse,
Peter M. Howley
(1994).
Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53..
Proceedings of the National Academy of Sciences
, 91
(19)
, 8797-8801.
https://doi.org/10.1073/pnas.91.19.8797
Identifiers
- DOI
- 10.1073/pnas.91.19.8797