ArticleProceedings of the National Academy of Sciences of the United States of America2005
The roles of the residues on the channel beta-hairpin and loop structures of simian virus 40 hexameric helicase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 57 citations in OpenAlex.
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- Cryo-EM structure of AAV2 Rep68 bound to integration site AAVS1: insights into the mechanism of DNA melting.Nucleic acids research · 2025Article
- A model for polyomavirus helicase activity derived in part from the AlphaFold2 structure of SV40 T-antigen.Journal of virology · 2024Article
- Cryo-EM Structure of AAV2 Rep68 bound to integration site AAVS1: Insights into the mechanism of DNA melting.bioRxiv : the preprint server for biology · 2024Article
- The Vaccinia Virus DNA Helicase Structure from Combined Single-Particle Cryo-Electron Microscopy and AlphaFold2 Prediction.Viruses · 2022Article
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- Replication of JC Virus DNA in the G144 Oligodendrocyte Cell Line Is Dependent Upon Akt.Journal of virology · 2017Article
- Study of SV40 large T antigen nucleotide specificity for DNA unwinding.Virology journal · 2017Article
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- Structural Elements Regulating AAA+ Protein Quality Control Machines.Frontiers in molecular biosciences · 2017Review
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- Structural Based Analyses of the JC Virus T-Antigen F258L Mutant Provides Evidence for DNA Dependent Conformational Changes in the C-Termini of Polyomavirus Origin Binding Domains.PLoS pathogens · 2016Article
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- Mechanism of origin DNA recognition and assembly of an initiator-helicase complex by SV40 large tumor antigen.Cell reports · 2013Article
- Analysis of the costructure of the simian virus 40 T-antigen origin binding domain with site I reveals a correlation between GAGGC spacing and spiral assembly.Journal of virology · 2013Article
- Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Origin DNA melting and unwinding in DNA replication.Current opinion in structural biology · 2010Review
- 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
- Hexameric helicase deconstructed: interplay of conformational changes and substrate coupling.Biophysical journal · 2010Article
- Conformational rearrangements of SV40 large T antigen during early replication events.Journal of molecular biology · 2010Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Simian virus 40 large tumor antigen is required for DNA unwinding during viral replication. The helicase-active form of large tumor antigen is a ring-shaped hexamer/double hexamer, which has a positively charged hexameric channel for interacting with DNA. On the hexameric channel surface are six beta-hairpin structures and loops, emanating from each of the six subunits. At the tips of the beta-hairpin and the loop structures are two ring-shaped residues, H513 and F459, respectively. Additionally, two positively charged residues, K512 and K516, are near the tip of the beta-hairpin. The positions of these ring-shaped and positively charged residues suggest that they may play a role in binding DNA for helicase function. To understand the roles of these residues in helicase function, we obtained a set of mutants and examined various activities, including oligomerization, ATPase, DNA binding, and helicase activities. We found that substitution of these residues by Ala abolished helicase activity. Extensive mutagenesis showed that substitutions by ring-shaped residues (W and Y) at position F459 and by residues with hydrophobic or long aliphatic side chains (W, Y, F, L, M, and R) at position H513 supported helicase activity. Our study demonstrated that the four residues (F459, H513, K512, and K516) play a critical role in interacting with DNA for helicase function. The results suggest a possible mechanism to explain how these residues, as well as the beta-hairpin and the loop structures on which the residues reside, participate in binding and translocating DNA for origin melting and unwinding.
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