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Science 28 July 1995: Vol. 269. no. 5223, pp. 529 - 531 DOI: 10.1126/science.7624774
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Articles
Science, Vol 269, Issue 5223, 529-531
Copyright © 1995 by American Association for the Advancement of Science
Interaction of papillomavirus E6 oncoproteins with a putative calcium-binding protein
JJ Chen,
CE Reid,
V Band,
and
EJ Androphy
Department of Dermatology, New England Medical Center, Boston, MA, USA.
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 E6-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.
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