Interaction with CBP/p300 enables the bovine papillomavirus type 1 E6 oncoprotein to downregulate CBP/p300-mediated transactivation by p53

H. Zimmermann, C. H. Koh, R. Degenkolbe, M. J. O'Connor, A. Muller, G. Steger, J. J. Chen, Y. Lui, Elliot Androphy, H. U. Bernard

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

The E6 oncoprotein of bovine papillomavirus type 1 (BPV-1) can transform cells independently of p53 degradation. The precise mechanisms underlying this transformation are not yet completely understood. Here it is shown that BPV-1 E6 interacts with CBP/p300 in the same way as described for the E6 proteins of oncogenic human papillomaviruses. This interaction results in an inhibition of the transcriptional coactivator function of CBP/p300 required by p53 and probably by other transcription factors. The comparison of the CBP/p300-binding properties of BPV-1 E6 mutants previously characterized in transcription and transformation studies suggests (i) that the E6-CBP/p300 interaction may be necessary, but not sufficient, for cell transformation, and (ii) that the transcriptional activator function, inherent to the E6 protein, is not derived from forming a complex with CBP/p300.

Original languageEnglish (US)
Pages (from-to)2617-2623
Number of pages7
JournalJournal of General Virology
Volume81
Issue number11
StatePublished - 2000
Externally publishedYes

Fingerprint

Bovine papillomavirus 1
Oncogene Proteins
Transcriptional Activation
Down-Regulation
p300-CBP Transcription Factors
Activator Appliances
Proteins
Transcription Factors

ASJC Scopus subject areas

  • Virology
  • Immunology

Cite this

Zimmermann, H., Koh, C. H., Degenkolbe, R., O'Connor, M. J., Muller, A., Steger, G., ... Bernard, H. U. (2000). Interaction with CBP/p300 enables the bovine papillomavirus type 1 E6 oncoprotein to downregulate CBP/p300-mediated transactivation by p53. Journal of General Virology, 81(11), 2617-2623.

Interaction with CBP/p300 enables the bovine papillomavirus type 1 E6 oncoprotein to downregulate CBP/p300-mediated transactivation by p53. / Zimmermann, H.; Koh, C. H.; Degenkolbe, R.; O'Connor, M. J.; Muller, A.; Steger, G.; Chen, J. J.; Lui, Y.; Androphy, Elliot; Bernard, H. U.

In: Journal of General Virology, Vol. 81, No. 11, 2000, p. 2617-2623.

Research output: Contribution to journalArticle

Zimmermann, H, Koh, CH, Degenkolbe, R, O'Connor, MJ, Muller, A, Steger, G, Chen, JJ, Lui, Y, Androphy, E & Bernard, HU 2000, 'Interaction with CBP/p300 enables the bovine papillomavirus type 1 E6 oncoprotein to downregulate CBP/p300-mediated transactivation by p53', Journal of General Virology, vol. 81, no. 11, pp. 2617-2623.
Zimmermann, H. ; Koh, C. H. ; Degenkolbe, R. ; O'Connor, M. J. ; Muller, A. ; Steger, G. ; Chen, J. J. ; Lui, Y. ; Androphy, Elliot ; Bernard, H. U. / Interaction with CBP/p300 enables the bovine papillomavirus type 1 E6 oncoprotein to downregulate CBP/p300-mediated transactivation by p53. In: Journal of General Virology. 2000 ; Vol. 81, No. 11. pp. 2617-2623.
@article{ddad530df4d144e2bc6aeac20bc175b8,
title = "Interaction with CBP/p300 enables the bovine papillomavirus type 1 E6 oncoprotein to downregulate CBP/p300-mediated transactivation by p53",
abstract = "The E6 oncoprotein of bovine papillomavirus type 1 (BPV-1) can transform cells independently of p53 degradation. The precise mechanisms underlying this transformation are not yet completely understood. Here it is shown that BPV-1 E6 interacts with CBP/p300 in the same way as described for the E6 proteins of oncogenic human papillomaviruses. This interaction results in an inhibition of the transcriptional coactivator function of CBP/p300 required by p53 and probably by other transcription factors. The comparison of the CBP/p300-binding properties of BPV-1 E6 mutants previously characterized in transcription and transformation studies suggests (i) that the E6-CBP/p300 interaction may be necessary, but not sufficient, for cell transformation, and (ii) that the transcriptional activator function, inherent to the E6 protein, is not derived from forming a complex with CBP/p300.",
author = "H. Zimmermann and Koh, {C. H.} and R. Degenkolbe and O'Connor, {M. J.} and A. Muller and G. Steger and Chen, {J. J.} and Y. Lui and Elliot Androphy and Bernard, {H. U.}",
year = "2000",
language = "English (US)",
volume = "81",
pages = "2617--2623",
journal = "Journal of General Virology",
issn = "0022-1317",
publisher = "Society for General Microbiology",
number = "11",

}

TY - JOUR

T1 - Interaction with CBP/p300 enables the bovine papillomavirus type 1 E6 oncoprotein to downregulate CBP/p300-mediated transactivation by p53

AU - Zimmermann, H.

AU - Koh, C. H.

AU - Degenkolbe, R.

AU - O'Connor, M. J.

AU - Muller, A.

AU - Steger, G.

AU - Chen, J. J.

AU - Lui, Y.

AU - Androphy, Elliot

AU - Bernard, H. U.

PY - 2000

Y1 - 2000

N2 - The E6 oncoprotein of bovine papillomavirus type 1 (BPV-1) can transform cells independently of p53 degradation. The precise mechanisms underlying this transformation are not yet completely understood. Here it is shown that BPV-1 E6 interacts with CBP/p300 in the same way as described for the E6 proteins of oncogenic human papillomaviruses. This interaction results in an inhibition of the transcriptional coactivator function of CBP/p300 required by p53 and probably by other transcription factors. The comparison of the CBP/p300-binding properties of BPV-1 E6 mutants previously characterized in transcription and transformation studies suggests (i) that the E6-CBP/p300 interaction may be necessary, but not sufficient, for cell transformation, and (ii) that the transcriptional activator function, inherent to the E6 protein, is not derived from forming a complex with CBP/p300.

AB - The E6 oncoprotein of bovine papillomavirus type 1 (BPV-1) can transform cells independently of p53 degradation. The precise mechanisms underlying this transformation are not yet completely understood. Here it is shown that BPV-1 E6 interacts with CBP/p300 in the same way as described for the E6 proteins of oncogenic human papillomaviruses. This interaction results in an inhibition of the transcriptional coactivator function of CBP/p300 required by p53 and probably by other transcription factors. The comparison of the CBP/p300-binding properties of BPV-1 E6 mutants previously characterized in transcription and transformation studies suggests (i) that the E6-CBP/p300 interaction may be necessary, but not sufficient, for cell transformation, and (ii) that the transcriptional activator function, inherent to the E6 protein, is not derived from forming a complex with CBP/p300.

UR - http://www.scopus.com/inward/record.url?scp=0033756617&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033756617&partnerID=8YFLogxK

M3 - Article

VL - 81

SP - 2617

EP - 2623

JO - Journal of General Virology

JF - Journal of General Virology

SN - 0022-1317

IS - 11

ER -