Sequence-specific and general transcriptional activation by the bovine papillomavirus-1 E2 trans-activator require an N-terminal amphipathic helix-containing E2 domain

T H Haugen; L P Turek; F M Mercurio; T P Cripe; B J Olson; R D Anderson; D Seidl; M Karin; John Schiller

doi:10.1002/j.1460-2075.1988.tb03322.x

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Sequence-specific and general transcriptional activation by the bovine papillomavirus-1 E2 trans-activator require an N-terminal amphipathic helix-containing E2 domain

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Sequence-specific and general transcriptional activation by the bovine papillomavirus-1 E2 trans-activator require an N-terminal amphipathic helix-containing E2 domain

T H Haugen, L P Turek, F M Mercurio, T P Cripe, B J Olson, R D Anderson, D Seidl, M Karin and John Schiller

The EMBO journal, Vol.7(13), pp.4245-4253

12/20/1988

DOI: 10.1002/j.1460-2075.1988.tb03322.x

PMID: 2854060

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Abstract

The sequence-specific trans-activator protein of bovine papillomavirus (BPV)-1, E2, strongly increases transcription at promoters containing papillomaviral ACCG(N)4CGGT (E2P) cis motifs, but can also activate a wide range of co-transfected promoters without E2P cores to a lower extent. Analysis of multiple E2 mutants in transfected cells revealed that the C-terminal DNA binding E2 domain binds to the E2P cis sequences in the form of pre-existing nuclear dimers. The DNA binding function of E2 was required for specific trans-activation of the E2P elements, as well as for the function of the previously described C-terminal 'short E2' transrepressor. In addition to the C terminus, specific trans-activation also required an intact N-terminal half of the E2 protein. When expressed alone, the N-terminal E2 domain was found to activate heterologous promoters without E2P elements to an extent comparable to wild-type E2, and therefore represents the functional transcription activation domain of the E2 factor. In contrast to other DNA-binding activator proteins described to date, the transcriptional activation by the E2 factor can occur without specific DNA binding. Its mechanism may thus involve protein--protein interactions between common transcription factors and the N-terminal E2 domain which contains amphipathic helix motifs.

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Title: Subtitle: Sequence-specific and general transcriptional activation by the bovine papillomavirus-1 E2 trans-activator require an N-terminal amphipathic helix-containing E2 domain
Creators: T H Haugen - Department of Pathology, VAMC, Iowa City, IA
L P Turek - Department of Pathology, VAMC, Iowa City, IA
F M Mercurio - Department of Pathology, VAMC, Iowa City, IA
T P Cripe - Department of Pathology, VAMC, Iowa City, IA
B J Olson - Department of Pathology, VAMC, Iowa City, IA
R D Anderson - Department of Pathology, VAMC, Iowa City, IA
D Seidl - Department of Pathology, VAMC, Iowa City, IA
M Karin - Department of Pathology, VAMC, Iowa City, IA
John Schiller - Department of Pathology, VAMC, Iowa City, IA
Resource Type: Journal article
Publication Details: The EMBO journal, Vol.7(13), pp.4245-4253
DOI: 10.1002/j.1460-2075.1988.tb03322.x
PMID: 2854060
NLM abbreviation: EMBO J
ISSN: 0261-4189
eISSN: 1460-2075
Language: English
Date published: 12/20/1988
Academic Unit: Pathology
Record Identifier: 9984046808502771

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