ArticleNucleic acids research2023
The monomeric archaeal primase from Nanoarchaeum equitans harbours the features of heterodimeric archaeoeukaryotic primases and primes sequence-specifically.
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, 6 citations in OpenAlex.
- Phylogenetic and functional characterization of Asgard primases.Molecular biology and evolution · 2026Article
- A four-in-one replicase integrating key enzymatic activities for DNA replication.Nucleic acids research · 2025Article
- A mobile genetic element-derived primase-polymerase harbors multiple activities implicated in DNA replication and repair.Nucleic acids research · 2025Article
- Definition of the binding specificity of the T7 bacteriophage primase by analysis of a protein binding microarray using a thermodynamic model.Nucleic acids research · 2024Article
- Initial Primer Synthesis of a DNA Primase Monitored by Real-Time NMR Spectroscopy.Journal of the American Chemical Society · 2024Article
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3 authors at 1 institution in 1 country.
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Abstract
The marine thermophilic archaeon Nanoarchaeum equitans possesses a monomeric primase encompassing the conserved domains of the small catalytic and the large regulatory subunits of archaeoeukaryotic heterodimeric primases in one protein chain. The recombinant protein primes on templates containing a triplet with a central thymidine, thus displaying a pronounced sequence specificity typically observed with bacterial type primases only. The N. equitans primase (NEQ395) is a highly active primase enzyme synthesizing short RNA primers. Termination occurs preferentially at about nine nucleotides, as determined by HPLC analysis and confirmed with mass spectrometry. Possibly, the compact monomeric primase NEQ395 represents the minimal archaeoeukaryotic primase and could serve as a functional and structural model of the heterodimeric archaeoeukaryotic primases, whose study is hindered by engagement in protein assemblies and rather low activity.
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