ArticleProceedings of the National Academy of Sciences of the United States of America1994
The bovine papillomavirus E2 protein modulates the assembly of but is not stably maintained in a replication-competent multimeric E1-replication origin complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 85 citations in OpenAlex.
- Mechanisms of Viral DNA Replication of Human Papillomavirus: E2 Protein-Dependent Recruitment of E1 DNA Helicase to the Origin of DNA Replication.International journal of molecular sciences · 2025Article
- The SMC5/6 Complex Represses the Replicative Program of High-Risk Human Papillomavirus Type 31.Pathogens (Basel, Switzerland) · 2020Article
- A conserved regulatory module at the C terminus of the papillomavirus E1 helicase domain controls E1 helicase assembly.Journal of virology · 2015Article
- The E1 proteins.Virology · 2013Review
- CK2 phosphorylation inactivates DNA binding by the papillomavirus E1 and E2 proteins.Journal of virology · 2013Article
- Nuclear accumulation of the papillomavirus E1 helicase blocks S-phase progression and triggers an ATM-dependent DNA damage response.Journal of virology · 2011Article
- Nuclear export of human papillomavirus type 31 E1 is regulated by Cdk2 phosphorylation and required for viral genome maintenance.Journal of virology · 2010Article
- Development of quantitative and high-throughput assays of polyomavirus and papillomavirus DNA replication.Virology · 2010Article
- Topography of bovine papillomavirus E2 protein on the viral genome during the cell cycle.Virology · 2009Article
- A DNA-binding activity in BPV initiator protein E1 required for melting duplex ori DNA but not processive helicase activity initiated on partially single-stranded DNA.Nucleic acids research · 2008Article
- Recent advances in the search for antiviral agents against human papillomaviruses.Antiviral therapy · 2007Review
- Cellular topoisomerase I modulates origin binding by bovine papillomavirus type 1 E1.Journal of virology · 2006Article
- Common determinants in DNA melting and helicase-catalysed DNA unwinding by papillomavirus replication protein E1.Nucleic acids research · 2006Article
- The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2.Genes & development · 2004Article
- 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
- Sequential and ordered assembly of E1 initiator complexes on the papillomavirus origin of DNA replication generates progressive structural changes related to melting.Molecular and cellular biology · 2002Article
- Chaperone proteins abrogate inhibition of the human papillomavirus (HPV) E1 replicative helicase by the HPV E2 protein.Molecular and cellular biology · 2002Article
- Papillomavirus E1 proteins: form, function, and features.Virus genes · 2002Review
- Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex.The EMBO journal · 2002Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Initiation of bovine papillomavirus (BPV) DNA synthesis in vivo and in vitro depends on the interaction of the viral initiator protein E1 with the replication origin (ori+ DNA). The viral E2 protein assists this interaction, resulting in a cooperative assembly of both proteins on the replication origin. Using gel mobility-shift experiments, we demonstrate that in the presence of both E1 and E2 proteins two classes of ori+ DNA complexes were formed: complex 1 (c1) and complex 2 (c2). Formation of c1 depended on both the E1 and E2 proteins and both proteins were contained within c1. The generation of c2 was dependent on the E1 protein and could be enhanced by E2, but the E2 protein was not detected within c2. At high E2/E1 ratios, c1 was the dominant complex formed. Under these conditions, E1-dependent BPV DNA synthesis in vitro was inhibited. At low E2/E1 ratios, the stimulation of c2 was correlated with the stimulation of BPV DNA replication by E2 in vitro. These data suggest that E2 assists E1 in the formation of an intermediate c1 complex, which is replication inactive. The c1 complex is converted in turn to the replication-active c2 complex, which contains E1 but lacks E2. We propose that the ratios of c1 and c2 formed in response to the levels of E1 and E2 protein determine the potential for BPV DNA synthesis in vitro and in vivo and may contribute to copy number regulation of BPV plasmids within the cell.
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