ArticleJournal of virology1999
Two regions of simian virus 40 T antigen determine cooperativity of double-hexamer assembly on the viral origin of DNA replication and promote hexamer interactions during bidirectional origin DNA unwinding.
Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
53 citing papers in PubMed, 76 citations in OpenAlex.
- Single-cell analysis reveals host S phase drives large T antigen expression during BK polyomavirus infection.PLoS pathogens · 2024Article
- A model for polyomavirus helicase activity derived in part from the AlphaFold2 structure of SV40 T-antigen.Journal of virology · 2024Article
- Proteomics Analysis of the Polyomavirus DNA Replication Initiation Complex Reveals Novel Functional Phosphorylated Residues and Associated Proteins.International journal of molecular sciences · 2024Article
- SV40 T-antigen uses a DNA shearing mechanism to initiate origin unwinding.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- SV40 T antigen helicase domain regions responsible for oligomerisation regulate Okazaki fragment synthesis initiation.FEBS open bio · 2022Article
- 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
- Replication-fork dynamics.Cold Spring Harbor perspectives in biology · 2014Review
- 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
- ATM and ATR activities maintain replication fork integrity during SV40 chromatin replication.PLoS pathogens · 2013Article
- Article
- Modeling of the SV40 DNA Replication Machine.Genes · 2012Article
- Inhibition of human papillomavirus DNA replication by an E1-derived p80/UAF1-binding peptide.Journal of virology · 2012Article
- A wolf in sheep's clothing: SV40 co-opts host genome maintenance proteins to replicate viral DNA.PLoS pathogens · 2012Review
- 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
- Uncoupling of sister replisomes during eukaryotic DNA replication.Molecular cell · 2010Article
- Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site.Biochemistry · 2010Article
- Origin DNA melting and unwinding in DNA replication.Current opinion in structural biology · 2010Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Phosphorylation of simian virus 40 large tumor (T) antigen on threonine 124 is essential for viral DNA replication. A mutant T antigen (T124A), in which this threonine was replaced by alanine, has helicase activity, assembles double hexamers on viral-origin DNA, and locally distorts the origin DNA structure, but it cannot catalyze origin DNA unwinding. A class of T-antigen mutants with single-amino-acid substitutions in the DNA binding domain (class 4) has remarkably similar properties, although these proteins are phosphorylated on threonine 124, as we show here. By comparing the DNA binding properties of the T124A and class 4 mutant proteins with those of the wild type, we demonstrate that mutant double hexamers bind to viral origin DNA with reduced cooperativity. We report that T124A T-antigen subunits impair the ability of double hexamers containing the wild-type protein to unwind viral origin DNA, suggesting that interactions between hexamers are also required for unwinding. Moreover, the T124A and class 4 mutant T antigens display dominant-negative inhibition of the viral DNA replication activity of the wild-type protein. We propose that interactions between hexamers, mediated through the DNA binding domain and the N-terminal phosphorylated region of T antigen, play a role in double-hexamer assembly and origin DNA unwinding. We speculate that one surface of the DNA binding domain in each subunit of one hexamer may form a docking site that can interact with each subunit in the other hexamer, either directly with the N-terminal phosphorylated region or with another region that is regulated by phosphorylation.
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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.