ArticleJournal of virology2007
Quantitative analysis of the binding of simian virus 40 large T antigen to DNA.
Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- A model for polyomavirus helicase activity derived in part from the AlphaFold2 structure of SV40 T-antigen.Journal of virology · 2024Article
- SV40 T antigen interactions with ssDNA and replication protein A: a regulatory role of T antigen monomers in lagging strand DNA replication.Nucleic acids research · 2020Article
- Characterization of an HPV33 natural variant with enhanced transcriptional activity suggests a role for C/EBPβ in the regulation of the viral early promoter.Scientific reports · 2019Article
- 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
- Phosphorylation of Merkel cell polyomavirus large tumor antigen at serine 816 by ATM kinase induces apoptosis in host cells.The Journal of biological chemistry · 2015Article
- Insights into the initiation of JC virus DNA replication derived from the crystal structure of the T-antigen origin binding domain.PLoS pathogens · 2014Article
- Polyomavirus large T antigen binds symmetrical repeats at the viral origin in an asymmetrical manner.Journal of virology · 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
- Asymmetric assembly of Merkel cell polyomavirus large T-antigen origin binding domains at the viral origin.Journal of molecular biology · 2011Article
- A conserved amphipathic helix in the N-terminal regulatory region of the papillomavirus E1 helicase is required for efficient viral DNA replication.Journal of virology · 2011Article
- Structure-based design of a disulfide-linked oligomeric form of the simian virus 40 (SV40) large T antigen DNA-binding domain.Acta crystallographica. Section D, Biological crystallography · 2011Article
- Structure-based analysis of the interaction between the simian virus 40 T-antigen origin binding domain and single-stranded DNA.Journal of virology · 2011Article
- Conformational rearrangements of SV40 large T antigen during early replication events.Journal of molecular biology · 2010Article
- Development of quantitative and high-throughput assays of polyomavirus and papillomavirus DNA replication.Virology · 2010Article
- Characterization of papillomavirus E1 helicase mutants defective for interaction with the SUMO-conjugating enzyme Ubc9.Virology · 2009Article
- Regulation of gene expression by PrrA in Rhodobacter sphaeroides 2.4.1: role of polyamines and DNA topology.Journal of bacteriology · 2009Article
- Half-Site DNA sequence and spacing length contributions to PrrA binding to PrrA site 2 of RSP3361 in Rhodobacter sphaeroides 2.4.1.Journal of bacteriology · 2009Article
- Simian virus 40 large T antigen can specifically unwind the central palindrome at the origin of DNA replication.Journal of virology · 2009Article
- Systematic study of the functions for the residues around the nucleotide pocket in simian virus 40 AAA+ hexameric helicase.Journal of virology · 2008Article
- Human papillomavirus E1 helicase interacts with the WD repeat protein p80 to promote maintenance of the viral genome in keratinocytes.Journal of virology · 2008Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
SV40 large T antigen (T-ag) is a multifunctional protein that successively binds to 5'-GAGGC-3' sequences in the viral origin of replication, melts the origin, unwinds DNA ahead of the replication fork, and interacts with host DNA replication factors to promote replication of the simian virus 40 genome. The transition of T-ag from a sequence-specific binding protein to a nonspecific helicase involves its assembly into a double hexamer whose formation is likely dictated by the propensity of T-ag to oligomerize and its relative affinities for the origin as well as for nonspecific double- and single-stranded DNA. In this study, we used a sensitive assay based on fluorescence anisotropy to measure the affinities of wild-type and mutant forms of the T-ag origin-binding domain (OBD), and of a larger fragment containing the N-terminal domain (N260), for different DNA substrates. We report that the N-terminal domain does not contribute to binding affinity but reduces the propensity of the OBD to self-associate. We found that the OBD binds with different affinities to its four sites in the origin and determined a consensus binding site by systematic mutagenesis of the 5'-GAGGC-3' sequence and of the residue downstream of it, which also contributes to affinity. Interestingly, the OBD also binds to single-stranded DNA with an approximately 10-fold higher affinity than to nonspecific duplex DNA and in a mutually exclusive manner. Finally, we provide evidence that the sequence specificity of full-length T-ag is lower than that of the OBD. These results provide a quantitative basis onto which to anchor our understanding of the interaction of T-ag with the origin and its assembly into a double hexamer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.