Evidence map›Paper›PMID 24445805›Full record

ArticleNucleic acids research2014

A highly divergent archaeo-eukaryotic primase from the Thermococcus nautilus plasmid, pTN2.

Sukhvinder Gill, Mart Krupovic, Nicole Desnoues, Pierre Béguin, Guennadi Sezonov, Patrick Forterre

Open access · goldAbstract read
In one paragraph

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
5.9field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 30 citations in OpenAlex.

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  4. Current issues in molecular biology · 2022
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  11. Deep-sea vent phage DNA polymerase specifically initiates DNA synthesis in the absence of primers.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Review
  14. Article
  15. Archaeal extrachromosomal genetic elements.Microbiology and molecular biology reviews : MMBR · 2015
    Review
  16. Article
  17. The universal tree of life: an update.Frontiers in microbiology · 2015
    Review
  18. Article
  19. Article
  20. The SF1 helicase encoded by the archaeal plasmid pTN2 of Thermococcus nautili.Extremophiles : life under extreme conditions · 2014
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Sukhvinder GillInstitut Pasteur Unité Biologie Moléculaire du Gène chez les Extrêmophiles, 25 rue du Docteur Roux, 75015 Paris, France, CNRS UMR 7138 Systématique, Adaptation, Evolution, Université Paris 6 quai Saint-Bernard, 75252 Paris Cedex 05, France and Univ Paris-Sud Institut de Génétique et Microbiologie, CNRS UMR 8621, Orsay 91406, France.
Mart Krupovic
Nicole Desnoues
Pierre Béguin
Guennadi Sezonov
Patrick Forterre
Institut Pasteur · FRBiology of Extremophiles Laboratory · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report the characterization of a DNA primase/polymerase protein (PolpTN2) encoded by the pTN2 plasmid from Thermococcus nautilus. Sequence analysis revealed that this protein corresponds to a fusion between an N-terminal domain homologous to the small catalytic subunit PriS of heterodimeric archaeal and eukaryotic primases (AEP) and a C-terminal domain related to their large regulatory subunit PriL. This unique domain configuration is not found in other virus- and plasmid-encoded primases in which PriS-like domains are typically fused to different types of helicases. PolpTN2 exhibited primase, polymerase and nucleotidyl transferase activities and specifically incorporates dNTPs, to the exclusion of rNTPs. PolpTN2 could efficiently prime DNA synthesis by the T. nautilus PolB DNA polymerase, suggesting that it is used in vivo as a primase for pTN2 plasmid replication. The N-terminal PriS-like domain of PolpTN2 exhibited all activities of the full-length enzyme but was much less efficient in priming cellular DNA polymerases. Surprisingly, the N-terminal domain possesses reverse transcriptase activity. We speculate that this activity could reflect an ancestral function of AEP proteins in the transition from the RNA to the DNA world.

Indexed as

Amino Acid SequenceArchaeal ProteinsDNADNA-Directed DNA PolymeraseDNA PrimaseMolecular Sequence DataPlasmidsProtein Structure, TertiaryRNARNA-Directed DNA PolymeraseThermococcusArchaeal ProteinsDNADNA-Directed DNA PolymeraseDNA PrimaseRNARNA-Directed DNA PolymeraseRNA primers

Identifiers

PMID24445805
PMCPMC3973330
OpenAlexW2117136989

What OpenQuestion holds

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Registered trials

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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.