ArticleNucleic acids research2004
Assembly of the replication initiation complex on SV40 origin DNA.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
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- Proteomics Analysis of the Polyomavirus DNA Replication Initiation Complex Reveals Novel Functional Phosphorylated Residues and Associated Proteins.International journal of molecular sciences · 2024Article
- Phosphorylation of Human Polyomavirus Large and Small T Antigens: An Ignored Research Field.Viruses · 2023Review
- Intelligent nanotherapeutic strategies for the delivery of CRISPR system.Acta pharmaceutica Sinica. B · 2023Review
- The E1 proteins.Virology · 2013Review
- Functions of alternative replication protein A in initiation and elongation.Biochemistry · 2010Article
- Transient dsDNA breaks during pre-replication complex assembly.Nucleic acids research · 2009Article
- Proteins of the origin recognition complex (ORC) and DNA topoisomerases on mammalian chromatin.BMC molecular biology · 2009Article
- An alternative form of replication protein a prevents viral replication in vitro.The Journal of biological chemistry · 2009Article
- Systematic study of the functions for the residues around the nucleotide pocket in simian virus 40 AAA+ hexameric helicase.Journal of virology · 2008Article
- Identification of novel human Cdt1-binding proteins by a proteomics approach: proteolytic regulation by APC/CCdh1.Molecular biology of the cell · 2008Article
- Simian virus 40 DNA replication is dependent on an interaction between topoisomerase I and the C-terminal end of T antigen.Journal of virology · 2008Article
- Timed interactions between viral and cellular replication factors during the initiation of SV40 in vitro DNA replication.The Biochemical journal · 2007Article
- Different activities of the largest subunit of replication protein A cooperate during SV40 DNA replication.FEBS letters · 2007Article
- Human cytomegalovirus UL84 interacts with an RNA stem-loop sequence found within the RNA/DNA hybrid region of oriLyt.Journal of virology · 2007Article
- Role of the hydrophilic channels of simian virus 40 T-antigen helicase in DNA replication.Journal of virology · 2007Article
- Cellular topoisomerase I modulates origin binding by bovine papillomavirus type 1 E1.Journal of virology · 2006Article
- Epigenetic mechanisms affect mutant p53 transgene expression in WAP-mutp53 transgenic mice.Oncogene · 2005Article
- Insights into hRPA32 C-terminal domain--mediated assembly of the simian virus 40 replisome.Nature structural & molecular biology · 2005Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The assembly of the complex that forms over the simian virus 40 origin to initiate DNA replication is not well understood. This complex is composed of the virus-coded T antigen and three cellular proteins, replication protein A (RPA), DNA polymerase alpha/primase (pol/prim) and topoisomerase I (topo I) in association with the origin. The order in which these various proteins bind to the DNA was investigated by performing binding assays using biotinylated origin DNA. We demonstrate that in the presence of all four proteins, pol/prim was essential to stabilize the initiation complex from the disruptive effects of topo I. At the optimal concentration of pol/prim, topo I and RPA bound efficiently to the complex, although pol/prim itself was not detected in significant amounts. At higher concentrations less topo I was recruited, suggesting that DNA polymerase is an important modulator of the binding of topo I. Topo I, in turn, appeared to be involved in recruiting RPA. RPA, in contrast, seemed to have little or no effect on the recruitment of the other proteins to the origin. These and other data suggested that pol/prim is the first cellular protein to interact with the double-hexameric T antigen bound to the origin. This is likely followed by topo I and then RPA, or perhaps by a complex of topo I and RPA. Stoichiometric analysis of the topo I and T antigen present in the complex suggested that two molecules of topo I are recruited per double hexamer. Finally, we demonstrate that DNA has a role in recruiting topo I to the origin.
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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.