ArticleThe Journal of biological chemistry2014
The C-terminal domain of the DNA polymerase catalytic subunit regulates the primase and polymerase activities of the human DNA polymerase α-primase complex.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 38 citations in OpenAlex.
- The human primosome requires replication protein A when copying DNA with inverted repeats.Nucleic acids research · 2025Article
- New Progress on DNA Primase Subunit Enzymes Research and Link to Cancer Development and Treatment Approaches.Current cancer drug targets · 2025Review
- A mechanistic model of primer synthesis from catalytic structures of DNA polymerase α-primase.Nature structural & molecular biology · 2024Article
- Flexibility and Distributive Synthesis Regulate RNA Priming and Handoff in Human DNA Polymerase α-Primase.Journal of molecular biology · 2023Article
- Flexibility and distributive synthesis regulate RNA priming and handoff in human DNA polymerase α-primase.bioRxiv : the preprint server for biology · 2023Article
- Structures of human primosome elongation complexes.Nature structural & molecular biology · 2023Article
- Human DNA polymerase α has a strong mutagenic potential at the initial steps of DNA synthesis.Nucleic acids research · 2022Article
- Structural and Molecular Kinetic Features of Activities of DNA Polymerases.International journal of molecular sciences · 2022Review
- Kinetic investigation of the polymerase and exonuclease activities of human DNA polymerase ε holoenzyme.The Journal of biological chemistry · 2020Article
- An archaeal primase functions as a nanoscale caliper to define primer length.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Activity and fidelity of human DNA polymerase α depend on primer structure.The Journal of biological chemistry · 2018Article
- Functional and structural similarity of human DNA primase [4Fe4S] cluster domain constructs.PloS one · 2018Article
- Iron-Sulfur Clusters in DNA Polymerases and Primases of Eukaryotes.Methods in enzymology · 2018Article
- Crystal structure of the human Polϵ B-subunit in complex with the C-terminal domain of the catalytic subunit.The Journal of biological chemistry · 2017Article
- Comment on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".Science (New York, N.Y.) · 2017Article
- Monitoring the Retention of Human Proliferating Cell Nuclear Antigen at Primer/Template Junctions by Proteins That Bind Single-Stranded DNA.Biochemistry · 2017Article
- Replication Protein A Prohibits Diffusion of the PCNA Sliding Clamp along Single-Stranded DNA.Biochemistry · 2017Article
- Elaborated Action of the Human Primosome.Genes · 2017Review
- Article
- Mechanism of Concerted RNA-DNA Primer Synthesis by the Human Primosome.The Journal of biological chemistry · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The initiation of DNA synthesis during replication of the human genome is accomplished primarily by the DNA polymerase α-primase complex, which makes the RNA-DNA primers accessible to processive DNA pols. The structural information needed to understand the mechanism of regulation of this complex biochemical reaction is incomplete. The presence of two enzymes in one complex poses the question of how these two enzymes cooperate during priming of DNA synthesis. Yeast two-hybrid and direct pulldown assays revealed that the N-terminal domain of the large subunit of primase (p58N) directly interacts with the C-terminal domain of the catalytic subunit of polα (p180C). We found that a complex of the C-terminal domain of the catalytic subunit of polα with the second subunit (p180C-p70) stimulated primase activity, whereas the whole catalytically active heterodimer of polα (p180ΔN-p70) inhibited RNA synthesis by primase. Conversely, the polα catalytic domain without the C-terminal part (p180ΔN-core) possessed a much higher propensity to extend the RNA primer than the two-subunit polα (p180ΔN-p70), suggesting that p180C and/or p70 are involved in the negative regulation of DNA pol activity. We conclude that the interaction between p180C, p70, and p58 regulates the proper primase and polymerase function. The composition of the template DNA is another important factor determining the activity of the complex. We have found that polα activity strongly depends on the sequence of the template and that homopyrimidine runs create a strong barrier for DNA synthesis by polα.
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