ArticleJournal of virology2000
Two patches of amino acids on the E2 DNA binding domain define the surface for interaction with E1.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Phosphorylation of the Bovine Papillomavirus E2 Protein on Tyrosine Regulates Its Transcription and Replication Functions.Journal of virology · 2017Article
- A conserved regulatory module at the C terminus of the papillomavirus E1 helicase domain controls E1 helicase assembly.Journal of virology · 2015Article
- The papillomavirus E2 proteins.Virology · 2013Review
- Virology and molecular pathogenesis of HPV (human papillomavirus)-associated oropharyngeal squamous cell carcinoma.The Biochemical journal · 2012Review
- Evolutionary and biophysical relationships among the papillomavirus E2 proteins.Frontiers in bioscience (Landmark edition) · 2009Review
- Surface mutagenesis of the bovine papillomavirus E1 DNA binding domain reveals residues required for multiple functions related to DNA replication.Journal of virology · 2006Article
- Two heads are better than one: regulation of DNA replication by hexameric helicases.Genes & development · 2004Review
- Pathogenesis of human papillomaviruses in differentiating epithelia.Microbiology and molecular biology reviews : MMBR · 2004Review
- Characterization of the minimal DNA binding domain of the human papillomavirus e1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant protein.Journal of virology · 2003Article
- E1 initiator DNA binding specificity is unmasked by selective inhibition of non-specific DNA binding.The EMBO journal · 2003Article
- E1 protein of bovine papillomavirus type 1 interferes with E2 protein-mediated tethering of the viral DNA to mitotic chromosomes.Journal of virology · 2002Article
- Functional mapping of the DNA binding domain of bovine papillomavirus E1 protein.Journal of virology · 2001Article
- Separate domains in E1 and E2 proteins serve architectural and productive roles for cooperative DNA binding.The EMBO journal · 2000Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The E1 and E2 proteins from bovine papillomavirus bind cooperatively to the viral origin of DNA replication (ori), forming a complex which is essential for initiation of DNA replication. Cooperative binding has two components, in which (i) the DNA binding domains (DBDs) of the two proteins interact with each other and (ii) the E2 transactivation domain interacts with the helicase domain of E1. By generating specific point mutations in the DBD of E2, we have defined two patches of amino acids that are involved in the interaction with the E1 DBD. These same mutations, when introduced into the viral genome, result in severely reduced replication of the viral genome, as well as failure to transform mouse cells in tissue culture. Thus, the interaction between the E1 and E2 DBDs is important for the establishment of the viral genome as an episome and most likely contributes to the formation of a preinitiation complex on the viral ori.
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