DIMERIZATION OF THE HUMAN PAPILLOMAVIRUS E7 ONCOPROTEIN IN-VIVO

被引:52
作者
CLEMENS, KE
BRENT, R
GYURIS, J
MUNGER, K
机构
[1] HARVARD UNIV,SCH MED,DEPT PATHOL,BOSTON,MA 02115
[2] NCI,MOLEC VIROL LAB,BETHESDA,MD 20892
[3] MASSACHUSETTS GEN HOSP,DEPT MOLEC BIOL,BOSTON,MA 02114
[4] HARVARD UNIV,SCH MED,DEPT GENET,BOSTON,MA 02115
关键词
D O I
10.1006/viro.1995.9926
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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. (C) 1995 Academic Press, Inc.
引用
收藏
页码:289 / 293
页数:5
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