Dimerization of the human papillomavirus E7 oncoprotein in vivo.
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.
Laboratory of Molecular Virology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
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Clemens
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Brent
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Gyuris
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Münger
D000595:Amino Acid Sequence; D001665:Binding Sites; D001704:Biopolymers; D003545:Cysteine / Q000378:metabolism; D006801:Humans; D008670:Metals / Q000378:metabolism; D008969:Molecular Sequence Data; D009856:Oncogene Proteins, Viral / Q000378:metabolism*; D050725:Papillomavirus E7 Proteins; D013329:Structure-Activity Relationship; D015533:Transcriptional Activation; D015003:Yeasts
D001704:Biopolymers; D008670:Metals; D009856:Oncogene Proteins, Viral; D050725:Papillomavirus E7 Proteins; C059731:oncogene protein E7, Human papillomavirus type 16; D003545:Cysteine