ArticleMolecular and cellular biology1997
Denaturation of the simian virus 40 origin of replication mediated by human replication protein A.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- A comparative study of protein-ssDNA interactions.NAR genomics and bioinformatics · 2021Article
- Replication protein A: directing traffic at the intersection of replication and repair.Frontiers in bioscience (Landmark edition) · 2010Review
- Structural mechanism of RPA loading on DNA during activation of a simple pre-replication complex.The EMBO journal · 2006Article
- Formation of a complex between nucleolin and replication protein A after cell stress prevents initiation of DNA replication.The Journal of cell biology · 2000Article
- Hypoxia blocks in vivo initiation of simian virus 40 replication at a stage preceding origin unwinding.Journal of virology · 1999Article
- In vitro analysis of the zinc-finger motif in human replication protein A.The Biochemical journal · 1999Article
- Identification and characterization of the fourth single-stranded-DNA binding domain of replication protein A.Molecular and cellular biology · 1998Article
- The origin DNA-binding and single-stranded DNA-binding domains of simian virus 40 large T antigen are distinct.Journal of virology · 1998Article
- Promoter opening via a DNA fork junction binding activity.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Distinct roles of two binding sites for the bovine papillomavirus (BPV) E2 transactivator on BPV DNA replication.Journal of virology · 1998Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The initiation of simian virus 40 (SV40) replication requires recognition of the viral origin of replication (ori) by SV40 T antigen, followed by denaturation of ori in a reaction dependent upon human replication protein A (hRPA). To understand how origin denaturation is achieved, we constructed a 48-bp SV40 "pseudo-origin" with a central 8-nucleotide (nt) bubble flanked by viral sequences, mimicking a DNA structure found within the SV40 T antigen-ori complex. hRPA bound the pseudo-origin with similar stoichiometry and an approximately fivefold reduced affinity compared to the binding of a 48-nt single-stranded DNA molecule. The presence of hRPA not only distorted the duplex DNA flanking the bubble but also resulted in denaturation of the pseudo-origin substrate in an ATP-independent reaction. Pseudo-origin denaturation occurred in 7 mM MgCl2, distinguishing this reaction from Mg2+-independent DNA-unwinding activities previously reported for hRPA. Tests of other single-stranded DNA-binding proteins (SSBs) revealed that pseudo-origin binding correlates with the known ability of these SSBs to support the T-antigen-dependent origin unwinding activity. Our results suggest that hRPA binding to the T antigen-ori complex induces the denaturation of ori including T-antigen recognition sequences, thus releasing T antigen from ori to unwind the viral DNA. The denaturation activity of hRPA has the potential to play a significant role in other aspects of DNA metabolism, including DNA repair.
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