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

作者: M. Scheffner , J. M. Huibregtse , P. M. Howley

DOI: 10.1073/PNAS.91.19.8797

关键词: Ubiquitin-conjugating enzymeSubfamilySequence alignmentBiologyPeptide sequenceBiochemistryComplementary DNAUbiquitin-Protein LigasesArabidopsisUbiquitin

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

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