INTERACTION OF PAPILLOMAVIRUS E6 ONCOPROTEINS WITH A PUTATIVE CALCIUM-BINDING PROTEIN

被引：244

作者：

CHEN, JJ

REID, CE

BAND, V

ANDROPHY, EJ

机构：

[1] TUFTS UNIV NEW ENGLAND MED CTR, DEPT DERMATOL, BOSTON, MA 02111 USA

[2] TUFTS UNIV, SCH MED, BOSTON, MA 02111 USA

[3] TUFTS UNIV NEW ENGLAND MED CTR, DEPT RADIAT ONCOL, BOSTON, MA 02111 USA

[4] TUFTS UNIV NEW ENGLAND MED CTR, DEPT BIOCHEM, BOSTON, MA 02111 USA

[5] TUFTS UNIV NEW ENGLAND MED CTR, DEPT MOLEC BIOL & MICROBIOL, BOSTON, MA 02111 USA

来源：

SCIENCE | 1995年 / 269卷 / 5223期

关键词：

D O I：

10.1126/science.7624774

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：529 / 531

页数：3

共 40 条

[1] IDENTIFICATION OF THE HPV-16 E6 PROTEIN FROM TRANSFORMED MOUSE CELLS AND HUMAN CERVICAL-CARCINOMA CELL-LINES [J].