Open AccessPeptide Interactions Stabilize and Restructure Human Papillomavirus Type 16 E6 To Interact with p53
Author(s) -
Tina Ansari,
Nicole Brimer,
Scott Vande Pol
Publication year - 2012
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.01236-12
Subject(s) - ubiquitin ligase , adapter (computing) , biology , human papillomavirus , microbiology and biotechnology , ubiquitin , peptide , plasma protein binding , ubiquitin protein ligases , repressor , biochemistry , transcription factor , computer science , gene , medicine , operating system
Human papillomavirus type 16 (HPV-16) E6 (16E6) binds the E3 ubiquitin ligase E6AP and p53, thereby targeting degradation of p53 (M. Scheffner, B. A. Werness, J. M. Huibregtse, A. J. Levine, and P. M. Howley, Cell 63:1129–1136, 1990). Here we show that minimal 16E6-binding LXXLL peptides reshape 16E6 to confer p53 interaction and stabilize 16E6in vivo but that degradation of p53 by 16E6 requires E6AP expression. These experiments establish a general mechanism for how papillomavirus E6 binding to LXXLL peptides reshapes E6 to then act as an adapter molecule.
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