ArticleMolecular and cellular biology2002
Sequential and ordered assembly of E1 initiator complexes on the papillomavirus origin of DNA replication generates progressive structural changes related to melting.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Mechanisms of MCM2-7 helicase activation and initial DNA melting at near base-pair resolution.Nature communications · 2026Article
- HPV16 E2 protein possesses intrinsic helicase activity and sterically hinders E1 function through direct interaction.The Journal of biological chemistry · 2026Article
- Human Papillomavirus Replication Regulation by Acetylation of a Conserved Lysine in the E2 Protein.Journal of virology · 2018Article
- Article
- The E1 proteins.Virology · 2013Review
- CK2 phosphorylation inactivates DNA binding by the papillomavirus E1 and E2 proteins.Journal of virology · 2013Article
- Mechanistic analysis of local ori melting and helicase assembly by the papillomavirus E1 protein.Molecular cell · 2011Article
- 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
- Interferon-inducible protein, P56, inhibits HPV DNA replication by binding to the viral protein E1.The EMBO journal · 2008Article
- Functional mapping of the human papillomavirus type 16 E1 cistron.Journal of virology · 2008Article
- 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
- ATP-dependent minor groove recognition of TA base pairs is required for template melting by the E1 initiator protein.Journal of virology · 2007Article
- Surface mutagenesis of the bovine papillomavirus E1 DNA binding domain reveals residues required for multiple functions related to DNA replication.Journal of virology · 2006Article
- Common determinants in DNA melting and helicase-catalysed DNA unwinding by papillomavirus replication protein E1.Nucleic acids research · 2006Article
- Architecture of bacterial replication initiation complexes: orisomes from four unrelated bacteria.The Biochemical journal · 2005Article
- E1 initiator DNA binding specificity is unmasked by selective inhibition of non-specific DNA binding.The EMBO journal · 2003Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Multiple binding sites for an initiator protein are a common feature of replicator sequences from various organisms. By binding to the replicator, initiators mark the site and contribute to melting or distortion of the DNA by largely unknown mechanisms. Here we analyze origin of DNA replication (ori) binding by the E1 initiator and show sequential binding to a set of overlapping binding sites. The assembly of these initiator complexes is controlled by a gradual reduction in the dependence of interactions between the initiator and DNA and a gradual increase in the reliance on interactions between initiator molecules, providing a mechanism for sequential and orderly assembly. Importantly, the binding of the initiator causes progressive structural alterations both in the sites and in the sequences flanking the sites, eventually generating severe structural alterations. These results indicate that the process of template melting may be incremental, where binding of each initiator molecule serves as a wedge that upon binding gradually alters the template structure. This mechanism may explain the requirement for multiple initiator binding sites that is observed in many ori's.
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