ArticleNucleic acids research2018
The Zn-finger domain of human PrimPol is required to stabilize the initiating nucleotide during DNA priming.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Structural and mechanistic insights into primer synthesis initiation by DNA primase.Nature communications · 2026Article
- The 9-1-1 complex protects ssDNA gaps in BRCA2-deficient cancer.bioRxiv : the preprint server for biology · 2025Article
- Mouse PrimPol Outperforms Its Human Counterpart as a Robust DNA Primase.International journal of molecular sciences · 2025Article
- S-phase checkpoint protects from aberrant replication fork processing and degradation.Nucleic acids research · 2025Article
- Assembly and breakage of head-to-head double hexamer reveals mpox virus E5-catalyzed DNA unwinding initiation.Nature communications · 2025Article
- Archaeal replicative primase mediates DNA double-strand break repair.Nucleic acids research · 2025Article
- Decoding mitochondrial DNA damage and repair associated withFrontiers in cellular and infection microbiology · 2024Review
- 3'dNTP Binding Is Modulated during Primer Synthesis and Translesion by Human PrimPol.International journal of molecular sciences · 2023Article
- The role of catalytic and regulatory domains of human PrimPol in DNA binding and synthesis.Nucleic acids research · 2023Article
- Primase-polymerases: how to make a primer from scratch.Bioscience reports · 2023Review
- The enterohemorrhagic Escherichia coli insertion sequence-excision enhancer protein is a DNA polymerase with microhomology-mediated end-joining activity.Nucleic acids research · 2023Article
- Article
- PrimPol: A Breakthrough among DNA Replication Enzymes and a Potential New Target for Cancer Therapy.Biomolecules · 2022Review
- PLK1 regulates the PrimPol damage tolerance pathway during the cell cycle.Science advances · 2021Article
- Arabidopsis thaliana PrimPol is a primase and lesion bypass DNA polymerase with the biochemical characteristics to cope with DNA damage in the nucleus, mitochondria, and chloroplast.Scientific reports · 2021Article
- Article
- Structural basis of DNA synthesis opposite 8-oxoguanine by human PrimPol primase-polymerase.Nature communications · 2021Article
- The three-component helicase/primase complex of herpes simplex virus-1.Open biology · 2021Review
- Repriming DNA synthesis: an intrinsic restart pathway that maintains efficient genome replication.Nucleic acids research · 2021Review
- A unique arginine cluster in PolDIP2 enhances nucleotide binding and DNA synthesis by PrimPol.Nucleic acids research · 2021Article
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5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human PrimPol is a monomeric enzyme whose DNA primase activity is required to rescue stalled replication forks during nuclear and mitochondrial DNA replication. PrimPol contains an Archeal-Eukaryotic Primases (AEP) core followed by a C-terminal Zn finger-containing domain (ZnFD), that is exclusively required for primer formation and for PrimPol function in vivo. The present study describes the sequential substrate interactions of human PrimPol during primer synthesis, and the relevance of the ZnFD at each individual step. Both the formation of a PrimPol:ssDNA binary complex and the upcoming interaction with the 3'-nucleotide (pre-ternary complex) remained intact when lacking the ZnFD. Conversely, the ZnFD was required for the subsequent binding and selection of the 5'-nucleotide that will become the first nucleotide of the new primer strand. Providing different 5'-site nucleotides, we can conclude that the ZnFD of PrimPol most likely interacts with the γ-phosphate moiety of the 5'-site nucleotide, optimizing formation of the initial dimer. Moreover, the ZnFD also contributes to recognize the cryptic G at the preferred priming sequence 3'GTC5'. Dimer elongation to obtain long DNA primers occurs processively and is facilitated by the 5'-terminal triphosphate, indicating that the ZnFD is also essential in the subsequent translocation/elongation events during DNA primer synthesis.
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