ArticleJournal of virology2000
The simian virus 40 core origin contains two separate sequence modules that support T-antigen double-hexamer assembly.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Ring-shaped replicative helicase encircles double-stranded DNA during unwinding.Nucleic acids research · 2019Article
- Article
- Insights into the initiation of JC virus DNA replication derived from the crystal structure of the T-antigen origin binding domain.PLoS pathogens · 2014Article
- 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
- Quantitative analysis of the binding of simian virus 40 large T antigen to DNA.Journal of virology · 2007Article
- Model for T-antigen-dependent melting of the simian virus 40 core origin based on studies of the interaction of the beta-hairpin with DNA.Journal of virology · 2007Article
- The crystal structure of the SV40 T-antigen origin binding domain in complex with DNA.PLoS biology · 2007Article
- Crystal structure of the simian virus 40 large T-antigen origin-binding domain.Journal of virology · 2006Article
- Interactions required for binding of simian virus 40 T antigen to the viral origin and molecular modeling of initial assembly events.Journal of virology · 2004Article
- Assembly of the replication initiation complex on SV40 origin DNA.Nucleic acids research · 2004Article
- Nonspecific double-stranded DNA binding activity of simian virus 40 large T antigen is involved in melting and unwinding of the origin.Journal of virology · 2003Article
- Characterization of the DNA-binding properties of the origin-binding domain of simian virus 40 large T antigen by fluorescence anisotropy.Journal of virology · 2003Article
- Peptides containing cyclin/Cdk-nuclear localization signal motifs derived from viral initiator proteins bind to DNA when unphosphorylated.Journal of virology · 2002Article
- Preformed hexamers of SV40 T antigen are active in RNA and origin-DNA unwinding.Nucleic acids research · 2002Article
- Mutational analysis of simian virus 40 T-antigen primosome activities in viral DNA replication.Journal of virology · 2002Article
- In the simian virus 40 in vitro replication system, start site selection by the polymerase alpha-primase complex is not significantly altered by changes in the concentration of ribonucleotides.Journal of virology · 2001Article
- Phosphorylation of simian virus 40 T antigen on Thr 124 selectively promotes double-hexamer formation on subfragments of the viral core origin.Journal of virology · 2000Article
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5 authors.
Funding
Abstract
Using subfragments of the simian virus 40 (SV40) core origin, we demonstrate that two alternative modules exist for the assembly of T-antigen (T-ag) double hexamers. Pentanucleotides 1 and 3 and the early palindrome (EP) constitute one assembly unit, while pentanucleotides 2 and 4 and the AT-rich region constitute a second, relatively weak, assembly unit. Related studies indicate that on the unit made up of pentanucleotide 1 and 3 and the EP assembly unit, the first hexamer forms on pentanucleotide 1 and that owing to additional protein-DNA and protein-protein interactions, the second hexamer is able to form on pentanucleotide 3. Oligomerization on the unit made up of pentanucleotide 2 and 4 and the AT-rich region is initiated by assembly of a hexamer on pentanucleotide 4; subsequent formation of the second hexamer takes place on pentanucleotide 2. Given that oligomerization on the SV40 origin is limited to double-hexamer formation, it is likely that only a single module is used for the initial assembly of T-ag double hexamers. Finally, we discuss the evidence that nucleotide hydrolysis is required for the remodeling events that result in the utilization of the second assembly unit.
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