ArticleNucleic acids research2023
The role of catalytic and regulatory domains of human PrimPol in DNA binding and synthesis.
Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Structural and mechanistic insights into primer synthesis initiation by DNA primase.Nature communications · 2026Article
- Structural basis of herpesvirus helicase-primase inhibition by pritelivir and amenamevir.Science advances · 2025Article
- DNA synthesis across DNA hairpins by human PrimPol.DNA repair · 2024Article
- Genomic analysis of hyperparasitic viruses associated with entomopoxviruses.Virus evolution · 2024Article
- Primase-polymerases: how to make a primer from scratch.Bioscience reports · 2023Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Human PrimPol possesses DNA primase and DNA polymerase activities and restarts stalled replication forks protecting cells against DNA damage in nuclei and mitochondria. The zinc-binding motif (ZnFn) of the C-terminal domain (CTD) of PrimPol is required for DNA primase activity but the mechanism is not clear. In this work, we biochemically demonstrate that PrimPol initiates de novo DNA synthesis in cis-orientation, when the N-terminal catalytic domain (NTD) and the CTD of the same molecule cooperate for substrates binding and catalysis. The modeling studies revealed that PrimPol uses a similar mode of initiating NTP coordination as the human primase. The ZnFn motif residue Arg417 is required for binding the 5'-triphosphate group that stabilizes the PrimPol complex with a DNA template-primer. We found that the NTD alone is able to initiate DNA synthesis, and the CTD stimulates the primase activity of NTD. The regulatory role of the RPA-binding motif in the modulation of PrimPol binding to DNA is also demonstrated.
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Registered trials
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