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Dimerization of the human papillomavirus type 16 E2 N terminus results in DNA looping within the upstream regulatory region

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Dimerization of the human papillomavirus type 16 E2 N terminus results in DNA looping within the upstream regulatory region. / Hernandez-Ramon, Elena E.; Burns, Julie E.; Zhang, Wenke; Walker, Hannah F.; Allen, Stephanie; Antson, Alfred A.; Maitland, Norman J.

In: JOURNAL OF VIROLOGY, Vol. 82, No. 10, 05.2008, p. 4853-4861.

Research output: Contribution to journalArticle

Harvard

Hernandez-Ramon, EE, Burns, JE, Zhang, W, Walker, HF, Allen, S, Antson, AA & Maitland, NJ 2008, 'Dimerization of the human papillomavirus type 16 E2 N terminus results in DNA looping within the upstream regulatory region', JOURNAL OF VIROLOGY, vol. 82, no. 10, pp. 4853-4861. https://doi.org/10.1128/JVI.02388-07

APA

Hernandez-Ramon, E. E., Burns, J. E., Zhang, W., Walker, H. F., Allen, S., Antson, A. A., & Maitland, N. J. (2008). Dimerization of the human papillomavirus type 16 E2 N terminus results in DNA looping within the upstream regulatory region. JOURNAL OF VIROLOGY, 82(10), 4853-4861. https://doi.org/10.1128/JVI.02388-07

Vancouver

Hernandez-Ramon EE, Burns JE, Zhang W, Walker HF, Allen S, Antson AA et al. Dimerization of the human papillomavirus type 16 E2 N terminus results in DNA looping within the upstream regulatory region. JOURNAL OF VIROLOGY. 2008 May;82(10):4853-4861. https://doi.org/10.1128/JVI.02388-07

Author

Hernandez-Ramon, Elena E. ; Burns, Julie E. ; Zhang, Wenke ; Walker, Hannah F. ; Allen, Stephanie ; Antson, Alfred A. ; Maitland, Norman J. / Dimerization of the human papillomavirus type 16 E2 N terminus results in DNA looping within the upstream regulatory region. In: JOURNAL OF VIROLOGY. 2008 ; Vol. 82, No. 10. pp. 4853-4861.

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@article{ac40c87b89cc4c7ca3b3c3bc98478b60,
title = "Dimerization of the human papillomavirus type 16 E2 N terminus results in DNA looping within the upstream regulatory region",
abstract = "Papillomavirus E2 proteins play a central role in regulating viral gene expression and replication. DNA-binding activity is associated with the C-terminal domain of E2, which forms a stable dimer, while the N-terminal domain is responsible for E2's replication and transactivation functions. The crystal structure of the latter domain revealed a second dimerization interface on E2 which may be responsible for DNA loop formation in the regulatory region of the human papillomavirus (HPV) genome. We investigated the biological significance of the N-terminal dimerization by introducing single amino acid substitutions into the dimerization interface. As expected, these substitutions did not influence the C-terminal dimerization and DNA-binding functions of E2. However, the mutations led to reduced transactivation of a synthetic E2-responsive reporter gene, while HPV DNA replication was unaffected. The effect of the mutations on DNA looping was visualized by atomic force microscopy. While wild-type E2 was able to generate DNA loops, all three mutant E2 proteins were defective in this ability. Our results suggest that N-terminal dimerization plays a role in E2-mediated transactivation, probably via DNA looping, a common mechanism for remote regulation of gene transcription.",
keywords = "TRANSCRIPTIONAL ACTIVATION, TRANSACTIVATION DOMAIN, CRYSTAL-STRUCTURE, REPLICATION FUNCTIONS, BINDING DOMAIN, PROTEIN, BRD4, ASSOCIATION, MUTAGENESIS, REPRESSION",
author = "Hernandez-Ramon, {Elena E.} and Burns, {Julie E.} and Wenke Zhang and Walker, {Hannah F.} and Stephanie Allen and Antson, {Alfred A.} and Maitland, {Norman J.}",
year = "2008",
month = "5",
doi = "10.1128/JVI.02388-07",
language = "English",
volume = "82",
pages = "4853--4861",
journal = "JOURNAL OF VIROLOGY",
issn = "0022-538X",
publisher = "American Society for Microbiology",
number = "10",

}

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TY - JOUR

T1 - Dimerization of the human papillomavirus type 16 E2 N terminus results in DNA looping within the upstream regulatory region

AU - Hernandez-Ramon, Elena E.

AU - Burns, Julie E.

AU - Zhang, Wenke

AU - Walker, Hannah F.

AU - Allen, Stephanie

AU - Antson, Alfred A.

AU - Maitland, Norman J.

PY - 2008/5

Y1 - 2008/5

N2 - Papillomavirus E2 proteins play a central role in regulating viral gene expression and replication. DNA-binding activity is associated with the C-terminal domain of E2, which forms a stable dimer, while the N-terminal domain is responsible for E2's replication and transactivation functions. The crystal structure of the latter domain revealed a second dimerization interface on E2 which may be responsible for DNA loop formation in the regulatory region of the human papillomavirus (HPV) genome. We investigated the biological significance of the N-terminal dimerization by introducing single amino acid substitutions into the dimerization interface. As expected, these substitutions did not influence the C-terminal dimerization and DNA-binding functions of E2. However, the mutations led to reduced transactivation of a synthetic E2-responsive reporter gene, while HPV DNA replication was unaffected. The effect of the mutations on DNA looping was visualized by atomic force microscopy. While wild-type E2 was able to generate DNA loops, all three mutant E2 proteins were defective in this ability. Our results suggest that N-terminal dimerization plays a role in E2-mediated transactivation, probably via DNA looping, a common mechanism for remote regulation of gene transcription.

AB - Papillomavirus E2 proteins play a central role in regulating viral gene expression and replication. DNA-binding activity is associated with the C-terminal domain of E2, which forms a stable dimer, while the N-terminal domain is responsible for E2's replication and transactivation functions. The crystal structure of the latter domain revealed a second dimerization interface on E2 which may be responsible for DNA loop formation in the regulatory region of the human papillomavirus (HPV) genome. We investigated the biological significance of the N-terminal dimerization by introducing single amino acid substitutions into the dimerization interface. As expected, these substitutions did not influence the C-terminal dimerization and DNA-binding functions of E2. However, the mutations led to reduced transactivation of a synthetic E2-responsive reporter gene, while HPV DNA replication was unaffected. The effect of the mutations on DNA looping was visualized by atomic force microscopy. While wild-type E2 was able to generate DNA loops, all three mutant E2 proteins were defective in this ability. Our results suggest that N-terminal dimerization plays a role in E2-mediated transactivation, probably via DNA looping, a common mechanism for remote regulation of gene transcription.

KW - TRANSCRIPTIONAL ACTIVATION

KW - TRANSACTIVATION DOMAIN

KW - CRYSTAL-STRUCTURE

KW - REPLICATION FUNCTIONS

KW - BINDING DOMAIN

KW - PROTEIN

KW - BRD4

KW - ASSOCIATION

KW - MUTAGENESIS

KW - REPRESSION

UR - http://www.scopus.com/inward/record.url?scp=43249123540&partnerID=8YFLogxK

U2 - 10.1128/JVI.02388-07

DO - 10.1128/JVI.02388-07

M3 - Article

VL - 82

SP - 4853

EP - 4861

JO - JOURNAL OF VIROLOGY

JF - JOURNAL OF VIROLOGY

SN - 0022-538X

IS - 10

ER -