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.
Clemens
K E
KE
Laboratory of Molecular Virology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Brent
R
R
Gyuris
J
J
Münger
K
K
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