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J. Biol. Chem., Vol. 277, Issue 47, 45619-45629, November 22, 2002
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From the Department of Biochemistry, Case Western Reserve
University School of Medicine, Cleveland, Ohio 44106-4935
The full-length E2 protein, encoded by
human papillomaviruses (HPVs), is a sequence-specific transcription
factor found in all HPVs, including cancer-causing high risk HPV types
16 and 18 and wart-inducing low risk HPV types 6 and 11. To investigate whether E2 proteins encoded by high risk HPVs may function
differentially from E2 proteins encoded by low risk HPVs and animal
papillomaviruses, we conducted comparative DNA-binding and
transcription studies using electrophoretic mobility shift assays and
cell-free transcription systems reconstituted with purified general
transcription factors, cofactor, RNA polymerase II, and with E2
proteins encoded by HPV-16, HPV-18, HPV-11, and bovine papillomavirus
type 1 (BPV-1). We found that although different types of E2 proteins
all exhibited transactivation and repression activities, depending on
the sequence context of the E2-binding sites, HPV-16 E2 shows stronger
transcription activity and greater DNA-binding affinity than those
displayed by the other E2 proteins. Surprisingly, HPV-18 E2 behaves
more similarly to BPV-1 E2 than HPV-16 E2 in its functional properties.
Our studies thus categorize HPV-18 E2 and BPV-1 E2 in the same protein
family, a finding consistent with the available E2 structural data that separate the closely related HPV-16 and HPV-18 E2 proteins but classify
together the more divergent BPV-1 and HPV-18 E2 proteins.
Transcriptional Activity among High and Low Risk Human
Papillomavirus E2 Proteins Correlates with E2 DNA Binding*
*
This work was supported by Grants CA81017 and GM59643 from
the National Institutes of Health and Grant RPG-97-135-04-MBC from the
American Cancer Society.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Mt. Sinai Health Care Foundation scholar. To whom correspondence
should be addressed: Dept. of Biochemistry, W-409, Case Western Reserve
University School of Medicine, 10900 Euclid Ave., Cleveland, OH
44106-4935. Tel.: 216-368-8550; Fax: 216-368-3419; E-mail: c-chiang@biochemistry.cwru.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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