ArticleJournal of virology2008
Dimerization of the human papillomavirus type 16 E2 N terminus results in DNA looping within the upstream regulatory region.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- In Silico Identification of Potential Antagonists Targeting the HPV16 E2-E1 Interaction: A Step Toward Novel Therapeutics for Cervical Cancer.Current issues in molecular biology · 2025Article
- A conserved cysteine in the DNA-binding domain of MmuPV1 E2 is required for replicationJournal of virology · 2025Article
- Preclinical Immunogenicity and Efficacy Studies for Therapeutic Vaccines for Human Papillomavirus-Type-16-Associated Cancer.Vaccines · 2024Article
- Sequence-Dependent Interaction of the Human Papillomavirus E2 Protein with the DNA Elements on Its DNA Replication Origin.International journal of molecular sciences · 2023Article
- The papillomavirus E2 proteins.Virology · 2013Review
- Genetic analysis of the E2 transactivation domain dimerization interface from bovine papillomavirus type 1.Virology · 2013Article
- A point mutation in the DNA-binding domain of HPV-2 E2 protein increases its DNA-binding capacity and reverses its transcriptional regulatory activity on the viral early promoter.BMC molecular biology · 2012Article
- Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site.Biochemistry · 2010Article
- Zinc coordination is required for and regulates transcription activation by Epstein-Barr nuclear antigen 1.PLoS pathogens · 2009Article
- Dimerization of the papillomavirus E2 protein is required for efficient mitotic chromosome association and Brd4 binding.Journal of virology · 2008Article
- Replication and partitioning of papillomavirus genomes.Advances in virus research · 2008Review
- Tumor suppressor or oncogene? A critical role of the human papillomavirus (HPV) E2 protein in cervical cancer progression.American journal of cancer researchArticle
Corrections and comments
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Authors and funding
7 authors.
Funding
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.
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