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Homologous sequences in adenovirus E1A and human papillomavirus E7 proteins mediate interaction with the same set of cellular proteins

Dyson, N, Guida, P, Münger, K, Harlow, E·1992·Journal of Virology
DOI 10.1128/jvi.66.12.6893-6902.1992
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Abstract

Studies of adenovirus E1A oncoprotein mutants suggest that the association of E1A with the retinoblastoma protein (pRB) is necessary for E1A-mediated transformation. Mutational analysis of E1A indicates that two regions of pRB are required for E1A to form stable complexes with the retinoblastoma protein. In addition to pRB binding, these regions are necessary for E1A association with several other cellular proteins, including p130, p107, cyclin A, and p33cdk2. Here we show that short synthetic peptides containing the pRB-binding sequences of E1A are sufficient for interaction with p107, cyclin A, and p130. The E7 protein of human papillomavirus type 16 contains an element that binds to pRB and appears to be functionally homologous to the E1A sequences. Peptides containing this region of the E7 protein were able to interact with p107, cyclin A, and p130 in addition to pRB. These findings suggest that the common mechanism of transformation used by these viral oncogenes involves their association with a set of polypeptides.

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Metadata

Authors
Dyson, N., Guida, P., Münger, K., & Harlow, E.
Affiliations
Massachusetts General Hospital Cancer Center, Charlestown 02129.
Venue
Journal of Virology
Publisher
American Society for Microbiology
Published
1992-12
Volume
66
Issue
12
Pages
6893-6902
ISSN
  • 0022-538X
  • 1098-5514
DOI
10.1128/jvi.66.12.6893-6902.1992
Cited by
314
References
4
Language
en
Licence
journals.asm.org/non-commercial-tdm-license (tdm)

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