ArticleProceedings of the National Academy of Sciences of the United States of America2012
Molecular interactions in the priming complex of bacteriophage T7.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. 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, 16 citations in OpenAlex.
- Primase promotes the competition between transcription and replication on the same template strand resulting in DNA damage.Nature communications · 2024Article
- Residues located in the primase domain of the bacteriophage T7 primase-helicase are essential for loading the hexameric complex onto DNA.The Journal of biological chemistry · 2022Article
- Arabidopsis thaliana organelles mimic the T7 phage DNA replisome with specific interactions between Twinkle protein and DNA polymerases Pol1A and Pol1B.BMC plant biology · 2019Article
- The application of thermophilic DNA primase TtDnaG2 to DNA amplification.Scientific reports · 2017Article
- Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Hybrid Methods Reveal Multiple Flexibly Linked DNA Polymerases within the Bacteriophage T7 Replisome.Structure (London, England : 1993) · 2017Article
- Stability versus exchange: a paradox in DNA replication.Nucleic acids research · 2016Article
- The DNA helicase-primase complex as a target for herpes viral infection.Expert opinion on therapeutic targets · 2013Review
- Discrete interactions between bacteriophage T7 primase-helicase and DNA polymerase drive the formation of a priming complex containing two copies of DNA polymerase.Biochemistry · 2013Article
- An interaction between DNA polymerase and helicase is essential for the high processivity of the bacteriophage T7 replisome.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The lagging-strand DNA polymerase requires an oligoribonucleotide, synthesized by DNA primase, to initiate the synthesis of an Okazaki fragment. In the replication system of bacteriophage T7 both DNA primase and DNA helicase activities are contained within a single protein, the bifunctional gene 4 protein (gp4). Intermolecular interactions between gp4 and T7 DNA polymerase are crucial for the stabilization of the oligoribonucleotide, its transfer to the polymerase, and its extension by DNA polymerase. We have identified conditions necessary to assemble the T7 priming complex and characterized its biophysical properties using fluorescence anisotropy. In order to reveal molecular interactions that occur during delivery of the oligoribonucleotide to DNA polymerase, we have used four genetically altered gp4 to demonstrate that both the RNA polymerase and the zinc-finger domains of DNA primase are involved in the stabilization of the priming complex and in sequence recognition in the DNA template. We find that the helicase domain of gp4 contributes to the stability of the complex by binding to the ssDNA template. The C-terminal tail of gp4 is not required for complex formation.
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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.