Identification of an α helical motif sufficient for association with papillomavirus E6

Jason J. Chen, Yihui Hong, Edward Rustamzadeh, James D. Baleja, Elliot J. Androphy

Research output: Contribution to journalArticle

84 Scopus citations

Abstract

We recently identified a cellular protein named E6BP or ERC-55 that binds cancer-related papillomavirus E6 proteins (Chen, J. J., Reid, C. E., Band, V., and Androphy, E. J. (1995) Science 269, 529-531). By construction of a series of deletion mutants, the region of E6BP that is necessary and sufficient for complex formation with human papillomavirus type 16 E6 has been mapped to a 25-amino acid domain. The corresponding peptide was synthesized and found by nuclear magnetic resonance spectroscopy to bind calcium and fold into a classical helix-loop-helix EF-hand conformation. Additional deletion mutagenesis showed that 13 amino acids that form the second α helix mediated E6 association. Alanine replacement mutagenesis indicated that amino acids of this helix were most important for E6 binding. Alignment of this α helical E6 binding peptide with the 18-amino acid E6 binding region of E6AP (Hulbregtse, J. M., Scheffner, M., and Howley, P.M. (1993) Mol. Cell Biol. 13, 4918-4927) and the first LD repeat of another E6- binding protein, paxillin (Tong, X., and Howley, P.M. (1997) J. Biol. Chem. 272, 33373-33376), revealed substantial similarities among these E6 binding domains. The extent of homology and the mutational data define the peptide as an E6 binding motif.

Original languageEnglish (US)
Pages (from-to)13537-13544
Number of pages8
JournalJournal of Biological Chemistry
Volume273
Issue number22
DOIs
StatePublished - May 29 1998
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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