INTERACTION OF PAPILLOMAVIRUS E6 ONCOPROTEINS WITH A PUTATIVE CALCIUM-BINDING PROTEIN
INTERACTION OF PAPILLOMAVIRUS E6 ONCOPROTEINS WITH A PUTATIVE CALCIUM-BINDING PROTEIN
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DOI：
10.1126/science.7624774
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发表时间：
1995-07-28
期刊：
影响因子：
56.9
通讯作者：
ANDROPHY, EJ
中科院分区：
文献类型：
--
作者：
CHEN, JJ;REID, CE;ANDROPHY, EJ
人乳头瘤病毒（HPV）与大多数宫颈癌相关，并编码一种转化蛋白E6，与肿瘤抑制蛋白p53相互作用。由于E6具有p53非依赖性转化活性，因此我们利用酵母双杂交系统寻找其它的EG结合蛋白。一种这样的蛋白质E6 BP与癌症相关的HPV E6和牛乳头瘤病毒1型（BPV-1）E6相互作用。BPV-1 E6突变体的转化活性与其E6 BP结合能力相关。E6 BP与一种假定的钙结合蛋白ERC-55相同，ERC-55似乎定位于内质网中。
Human papillomaviruses (HPVs) are associated with the majority of cervical cancers and encode a transforming protein, E6, that interacts with the tumor suppressor protein p53. Because E6 has p53-independent transforming activity, the yeast two-hybrid system was used to search for other EG-binding proteins. One such protein, E6BP, interacted with cancer-associated HPV E6 and with bovine papillomavirus type 1 (BPV-1) E6. The transforming activity of BPV-1 E6 mutants correlated with their E6BP-binding ability. E6BP is identical to a putative calcium-binding protein, ERC-55, that appears to be localized in the endoplasmic reticulum.