ArticleJournal of molecular biology2018
Novel Families of Archaeo-Eukaryotic Primases Associated with Mobile Genetic Elements of Bacteria and Archaea.
Article in Journal of molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 38 citations in OpenAlex.
- Fidelity, specialization, and evolution of Paramecium PolX DNA polymerases involved in programmed double-strand break DNA repair.Nucleic acids research · 2025Article
- A four-in-one replicase integrating key enzymatic activities for DNA replication.Nucleic acids research · 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
- Article
- 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
- UG/Abi: a highly diverse family of prokaryotic reverse transcriptases associated with defense functions.Nucleic acids research · 2022Article
- The combined DNA and RNA synthetic capabilities of archaeal DNA primase facilitate primer hand-off to the replicative DNA polymerase.Nature communications · 2022Article
- Deletion of the primase-polymerases encoding gene, located in a mobile element inFrontiers in microbiology · 2022Article
- CRISPR-Associated Primase-Polymerases are implicated in prokaryotic CRISPR-Cas adaptation.Nature communications · 2021Article
- The three-component helicase/primase complex of herpes simplex virus-1.Open biology · 2021Review
- How cyanophage S-2L rejects adenine and incorporates 2-aminoadenine to saturate hydrogen bonding in its DNA.Nature communications · 2021Article
- Molecular Dissection of the Primase and Polymerase Activities of Deep-Sea Phage NrS-1 Primase-Polymerase.Frontiers in microbiology · 2021Article
- The LUCA and its complex virome.Nature reviews. Microbiology · 2020Review
- A thermostable DNA primase-polymerase from a mobile genetic element involved in defence against environmental DNA.Environmental microbiology · 2020Article
- Diversity and evolution of B-family DNA polymerases.Nucleic acids research · 2020Review
- Archaeal DNA Replication.Annual review of microbiology · 2020Review
- The replication machinery of LUCA: common origin of DNA replication and transcription.BMC biology · 2020Article
- The global distribution and evolutionary history of the pT26-2 archaeal plasmid family.Environmental microbiology · 2019Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Cellular organisms in different domains of life employ structurally unrelated, non-homologous DNA primases for synthesis of a primer for DNA replication. Archaea and eukaryotes encode enzymes of the archaeo-eukaryotic primase (AEP) superfamily, whereas bacteria uniformly use primases of the DnaG family. However, AEP genes are widespread in bacterial genomes raising questions regarding their provenance and function. Here, using an archaeal primase-polymerase PolpTN2 encoded by pTN2 plasmid as a seed for sequence similarity searches, we recovered over 800 AEP homologs from bacteria belonging to 12 highly diverse phyla. These sequences formed a supergroup, PrimPol-PV1, and could be classified into five novel AEP families which are characterized by a conserved motif containing an arginine residue likely to be involved in nucleotide binding. Functional assays confirm the essentiality of this motif for catalytic activity of the PolpTN2 primase-polymerase. Further analyses showed that bacterial AEPs display a range of domain organizations and uncovered several candidates for novel families of helicases. Furthermore, sequence and structure comparisons suggest that PriCT-1 and PriCT-2 domains frequently fused to the AEP domains are related to each other as well as to the non-catalytic, large subunit of archaeal and eukaryotic primases, and to the recently discovered PriX subunit of archaeal primases. Finally, genomic neighborhood analysis indicates that the identified AEPs encoded in bacterial genomes are nearly exclusively associated with highly diverse integrated mobile genetic elements, including integrative conjugative plasmids and prophages.
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Registered trials
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