ArticleNucleic acids research2014
Molecular dissection of the domain architecture and catalytic activities of human PrimPol.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
What it found
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Who cites it
78 citing papers in PubMed, 105 citations in OpenAlex.
- The polymerase milieu of human papillomavirus.Journal of virology · 2026Review
- TET2 loss triggers ssDNA gap accumulation and heightened PARP inhibitor sensitivity.Nature communications · 2026Article
- Structural and mechanistic insights into primer synthesis initiation by DNA primase.Nature communications · 2026Article
- Understanding single stranded DNA gaps: from formation to fate.The Biochemical journal · 2026Review
- A bacterial PrimPol-reverse transcriptase hybrid protein has a proofreading exonuclease activity that can be transferred to other reverse transcriptases.bioRxiv : the preprint server for biology · 2025Article
- Mouse PrimPol Outperforms Its Human Counterpart as a Robust DNA Primase.International journal of molecular sciences · 2025Article
- MRN-CtIP, EXO1, and DNA2-WRN/BLM act bidirectionally to process DNA gaps in PARPi-treated cells without strand cleavage.Genes & development · 2025Article
- Archaeal replicative primase mediates DNA double-strand break repair.Nucleic acids research · 2025Article
- Nucleic acid joining enzymes: biological functions and synthetic applications beyond DNA.The Biochemical journal · 2025Review
- Molecular mechanisms of DNA lesion and repair during antibody somatic hypermutation.Science China. Life sciences · 2024Review
- PRIMPOL ensures robust handoff between on-the-fly and post-replicative DNA lesion bypass.Nucleic acids research · 2024Article
- Role of Translesion DNA Synthesis in the Metabolism of Replication-associated Nascent Strand Gaps.Journal of molecular biology · 2024Review
- 3'dNTP Binding Is Modulated during Primer Synthesis and Translesion by Human PrimPol.International journal of molecular sciences · 2023Article
- Dynamics of loops surrounding the active site architecture in GH5_2 subfamily TfCel5A for cellulose degradation.Biotechnology for biofuels and bioproducts · 2023Article
- Reverse transcriptases prime DNA synthesis.Nucleic acids research · 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
- Molecular choreography of primer synthesis by the eukaryotic Pol α-primase.Nature communications · 2023Article
- Molecular choreography of primer synthesis by the eukaryotic Pol α-primase.bioRxiv : the preprint server for biology · 2023Article
- Implications of Translesion DNA Synthesis Polymerases on Genomic Stability and Human Health.Molecular and cellular biology · 2023Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
PrimPol is a primase-polymerase involved in nuclear and mitochondrial DNA replication in eukaryotic cells. Although PrimPol is predicted to possess an archaeo-eukaryotic primase and a UL52-like zinc finger domain, the role of these domains has not been established. Here, we report that the proposed zinc finger domain of human PrimPol binds zinc ions and is essential for maintaining primase activity. Although apparently dispensable for its polymerase activity, the zinc finger also regulates the processivity and fidelity of PrimPol's extension activities. When the zinc finger is disrupted, PrimPol becomes more promutagenic, has an altered translesion synthesis spectrum and is capable of faithfully bypassing cyclobutane pyrimidine dimer photolesions. PrimPol's polymerase domain binds to both single- and double-stranded DNA, whilst the zinc finger domain binds only to single-stranded DNA. We additionally report that although PrimPol's primase activity is required to restore wild-type replication fork rates in irradiated PrimPol-/- cells, polymerase activity is sufficient to maintain regular replisome progression in unperturbed cells. Together, these findings provide the first analysis of the molecular architecture of PrimPol, describing the activities associated with, and interplay between, its functional domains and defining the requirement for its primase and polymerase activities during nuclear DNA replication.
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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.