ArticleJournal of virology1998
Characterization of the DNA-binding domain of the bovine papillomavirus replication initiator E1.
Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- Thermodynamic variations at the HPV E1-E2 interface correlate with clinical risk groups: an in-silico analysis.Virology journal · 2026Article
- 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
- A model for polyomavirus helicase activity derived in part from the AlphaFold2 structure of SV40 T-antigen.Journal of virology · 2024Article
- The SMC5/6 Complex Represses the Replicative Program of High-Risk Human Papillomavirus Type 31.Pathogens (Basel, Switzerland) · 2020Article
- E2 protein is the major determinant of specificity at the human papillomavirus origin of replication.PloS one · 2019Article
- Development of Protein-Protein Interaction Inhibitors for the Treatment of Infectious Diseases.Advances in protein chemistry and structural biology · 2018Review
- Bacteriophage T5 gene D10 encodes a branch-migration protein.Scientific reports · 2016Article
- Genomic characterization of a novel Epsilonpapillomavirus associated with pigmented papillomas in a red deer (Cervus elaphus).Virus genes · 2016Article
- Assessing parallel gene histories in viral genomes.BMC evolutionary biology · 2016Article
- A conserved regulatory module at the C terminus of the papillomavirus E1 helicase domain controls E1 helicase assembly.Journal of virology · 2015Article
- Dynamic look at DNA unwinding by a replicative helicase.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Genomic characterisation of Felis catus papillomavirus 4, a novel papillomavirus detected in the oral cavity of a domestic cat.Virus genes · 2014Article
- Structure of the NS1 protein N-terminal origin recognition/nickase domain from the emerging human bocavirus.Journal of virology · 2013Article
- The E1 proteins.Virology · 2013Review
- The papillomavirus E2 proteins.Virology · 2013Review
- CK2 phosphorylation inactivates DNA binding by the papillomavirus E1 and E2 proteins.Journal of virology · 2013Article
- Structure-based mutational analysis of the bovine papillomavirus E1 helicase domain identifies residues involved in the nonspecific DNA binding activity required for double trimer formation.Journal of virology · 2010Article
- 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
- Replication and partitioning of papillomavirus genomes.Advances in virus research · 2008Review
- Mismatch Repair proteins are recruited to replicating DNA through interaction with Proliferating Cell Nuclear Antigen (PCNA).Nucleic acids research · 2008Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The bovine papillomavirus replication initiator protein E1 is an origin of replication (ori)-binding protein absolutely required for viral DNA replication. In the presence of the viral transcription factor E2, E1 binds to the ori and initiates DNA replication. To understand how the E1 initiator recognizes the ori and how E2 assists in this process, we have expressed and purified a 166-amino-acid fragment which corresponds to the minimal E1 DNA-binding domain (DBD). DNA binding studies using this protein demonstrate that the E1 DBD can bind to the palindromic E1 binding site in several forms but that binding of two monomers, each recognizing one half-site of the E1 palindrome, is the predominant form. This is reminiscent of the binding of the T-antigen DBD to the SV40 ori, and interestingly, the arrangement of E1 binding sites shows striking similarities to the arrangement of T-antigen binding sites in the SV40 ori even though the recognition sequences are unrelated. The E1 DBD is capable of interacting cooperatively with E2; however, the E2 DBD and not the E2 activation domain mediates this interaction. Furthermore, the E2 DBD stimulates binding of two monomers of the E1 DBD to the ori by binding cooperatively with one E1 monomer. Finally, we show that our results concerning the DNA-binding properties of the E1 DBD can be extended to full-length E1.
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