Abstract
We have used a yeast two-hybrid system to show that human papillomavirus E7 proteins can form oligomeric complexes in vivo. The carboxyl-terminal cysteine-rich metal-binding domain is critical for this activity although amino-terminal sequences also contribute to oligomerization. Our experiments also reveal that E7 possesses an intrinsic transcription activation activity in yeast, which resides in the amino terminus of the protein.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Biopolymers
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Cysteine / metabolism
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Humans
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Metals / metabolism
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Molecular Sequence Data
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Oncogene Proteins, Viral / metabolism*
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Papillomavirus E7 Proteins
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Structure-Activity Relationship
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Transcriptional Activation
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Yeasts
Substances
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Biopolymers
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Metals
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Oncogene Proteins, Viral
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Papillomavirus E7 Proteins
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oncogene protein E7, Human papillomavirus type 16
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Cysteine