ArticleThe Journal of biological chemistry2010
A specific docking site for DNA polymerase {alpha}-primase on the SV40 helicase is required for viral primosome activity, but helicase activity is dispensable.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- 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 helicase domain regions responsible for oligomerisation regulate Okazaki fragment synthesis initiation.FEBS open bio · 2022Article
- Targeted chromosomal Escherichia coli:dnaB exterior surface residues regulate DNA helicase behavior to maintain genomic stability and organismal fitness.PLoS genetics · 2021Article
- FAM111A induces nuclear dysfunction in disease and viral restriction.EMBO reports · 2021Article
- 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
- Contribution of DNA Replication to the FAM111A-Mediated Simian Virus 40 Host Range Phenotype.Journal of virology · 2019Article
- Bacterial DnaB helicase interacts with the excluded strand to regulate unwinding.The Journal of biological chemistry · 2017Article
- Elaborated Action of the Human Primosome.Genes · 2017Review
- Mechanism of Concerted RNA-DNA Primer Synthesis by the Human Primosome.The Journal of biological chemistry · 2016Article
- Crystal Structure of the Human Pol α B Subunit in Complex with the C-terminal Domain of the Catalytic Subunit.The Journal of biological chemistry · 2015Article
- The conserved core enzymatic activities and the distinct dynamics of polyomavirus large T antigens.Archives of biochemistry and biophysics · 2015Article
- False-positive TUNEL staining observed in SV40 based transgenic murine prostate cancer models.Transgenic research · 2013Article
- Structural basis for the interaction of a hexameric replicative helicase with the regulatory subunit of human DNA polymerase α-primase.The Journal of biological chemistry · 2012Article
- Human DNA helicase B (HDHB) binds to replication protein A and facilitates cellular recovery from replication stress.The Journal of biological chemistry · 2012Article
- Origin DNA melting and unwinding in DNA replication.Current opinion in structural biology · 2010Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Replication of simian virus 40 (SV40) DNA, a model for eukaryotic chromosomal replication, can be reconstituted in vitro using the viral helicase (large tumor antigen, or Tag) and purified human proteins. Tag interacts physically with two cellular proteins, replication protein A and DNA polymerase α-primase (pol-prim), constituting the viral primosome. Like the well characterized primosomes of phages T7 and T4, this trio of proteins coordinates parental DNA unwinding with primer synthesis to initiate the leading strand at the viral origin and each Okazaki fragment on the lagging strand template. We recently determined the structure of a previously unrecognized pol-prim domain (p68N) that docks on Tag, identified the p68N surface that contacts Tag, and demonstrated its vital role in primosome function. Here, we identify the p68N-docking site on Tag by using structure-guided mutagenesis of the Tag helicase surface. A charge reverse substitution in Tag disrupted both p68N-binding and primosome activity but did not affect docking with other pol-prim subunits. Unexpectedly, the substitution also disrupted Tag ATPase and helicase activity, suggesting a potential link between p68N docking and ATPase activity. To assess this possibility, we examined the primosome activity of Tag with a single residue substitution in the Walker B motif. Although this substitution abolished ATPase and helicase activity as expected, it did not reduce pol-prim docking on Tag or primosome activity on single-stranded DNA, indicating that Tag ATPase is dispensable for primosome activity in vitro.
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