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Papillomavirus E7 protein blocks pCAF's acetyltransferase, a p53 coactivator.

Women's Health Weekly

| September 04, 2003 | COPYRIGHT 2003 NewsRX. This material is published under license from the publisher through the Gale Group, Farmington Hills, Michigan.  All inquiries regarding rights should be directed to the Gale Group. (Hide copyright information)Copyright

2003 SEP 4 - (NewsRx.com & NewsRx.net) -- Papillomavirus E7 proteins react with pCAF's acetyltransferase domain, normally a coactivator of the p53 transcription factor.

According to a study from Canada, "Most cervical carcinomas express the E6 and E7 proteins of a high-risk human papillomavirus (HPV). These proteins affect growth control by interfering with the functions of cell regulatory proteins, promoting oncogenic transformation.

"A key target of E7 is the tumor suppressor protein pRb, which directly interacts with E7. However, binding to additional cellular regulatory proteins is clearly required for oncogenesis, as mutants of E7 have been identified that bind to pRb, yet fail to transform efficiently.

"Here we demonstrate the interaction of the HPVs 6, 16 and 18s E7 proteins with the pCAF acetyltransferase, which has been reported to function as a coactivator for a variety of transcription factors including p53. Mutation of a highly conserved leucine residue within the zinc finger region of HPV 16 E7 disrupts binding to pCAF and also impairs transformation and transcriptional activation. HPV ...

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