ReviewNucleic acids research2015
Primase-polymerases are a functionally diverse superfamily of replication and repair enzymes.
Review in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed.
- Phylogenetic and functional characterization of Asgard primases.Molecular biology and evolution · 2026Article
- Environmental distribution, physiology and genomic adaptations of arctic ammonia-oxidizing archaea.Frontiers in microbiology · 2026Article
- Isolation, characterization, and genomic analysis of a novel phage WSPA with lytic activity againstMicrobiology spectrum · 2025Article
- Assembly and breakage of head-to-head double hexamer reveals mpox virus E5-catalyzed DNA unwinding initiation.Nature communications · 2025Article
- Comparative genomics of native plasmids from plant pathogenic Gammaproteobacteria.DNA research : an international journal for rapid publication of reports on genes and genomes · 2025Article
- Archaeal replicative primase mediates DNA double-strand break repair.Nucleic acids research · 2025Article
- A mobile genetic element-derived primase-polymerase harbors multiple activities implicated in DNA replication and repair.Nucleic acids research · 2025Article
- Isolation and genomic analysis of phage BUCT551 against drug-resistantFrontiers in veterinary science · 2025Article
- Characterization of the novel cross-genus phage vB_SmaS_QH3 and evaluation of its antibacterial efficacy againstFrontiers in microbiology · 2025Article
- Metagenomic characterization of viruses and mobile genetic elements associated with the DPANN archaeal superphylum.Nature microbiology · 2024Article
- Initial Primer Synthesis of a DNA Primase Monitored by Real-Time NMR Spectroscopy.Journal of the American Chemical Society · 2024Article
- The unfolded protein response of the endoplasmic reticulum protects Caenorhabditis elegans against DNA damage caused by stalled replication forks.G3 (Bethesda, Md.) · 2024Article
- Molecular markers associated with resistance to squash leaf curl China virus and tomato leaf curl New Delhi virus in tropical pumpkin (Cucurbita moschata Duchesne ex Poir.) breeding line AVPU1426.Scientific reports · 2024Article
- Genomic analysis and characterization of bacteriophage vB_SpuS_NX263 infecting Salmonella enterica subsp. enterica serovar Pullorum.Archives of virology · 2023Article
- Primase-polymerases: how to make a primer from scratch.Bioscience reports · 2023Review
- The monomeric archaeal primase from Nanoarchaeum equitans harbours the features of heterodimeric archaeoeukaryotic primases and primes sequence-specifically.Nucleic acids research · 2023Article
- Reclassification of family A DNA polymerases reveals novel functional subfamilies and distinctive structural features.Nucleic acids research · 2023Article
- The enterohemorrhagic Escherichia coli insertion sequence-excision enhancer protein is a DNA polymerase with microhomology-mediated end-joining activity.Nucleic acids research · 2023Article
- Genomes of six viruses that infect Asgard archaea from deep-sea sediments.Nature microbiology · 2022Article
- Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Until relatively recently, DNA primases were viewed simply as a class of proteins that synthesize short RNA primers requisite for the initiation of DNA replication. However, recent studies have shown that this perception of the limited activities associated with these diverse enzymes can no longer be justified. Numerous examples can now be cited demonstrating how the term 'DNA primase' only describes a very narrow subset of these nucleotidyltransferases, with the vast majority fulfilling multifunctional roles from DNA replication to damage tolerance and repair. This article focuses on the archaeo-eukaryotic primase (AEP) superfamily, drawing on recently characterized examples from all domains of life to highlight the functionally diverse pathways in which these enzymes are employed. The broad origins, functionalities and enzymatic capabilities of AEPs emphasizes their previous functional misannotation and supports the necessity for a reclassification of these enzymes under a category called primase-polymerases within the wider functional grouping of polymerases. Importantly, the repositioning of AEPs in this way better recognizes their broader roles in DNA metabolism and encourages the discovery of additional functions for these enzymes, aside from those highlighted here.
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