Evidence map›Paper›PMID 29167441›Full record

ArticleNature communications2017

Primer synthesis by a eukaryotic-like archaeal primase is independent of its Fe-S cluster.

Sandro Holzer, Jiangyu Yan, Mairi L Kilkenny, Stephen D Bell, Luca Pellegrini

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Frontiers in plant science · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Archaeal DNA Replication.Annual review of microbiology · 2020
    Review
  15. Initiating DNA replication: a matter of prime importance.Biochemical Society transactions · 2019
    Review
  16. An archaeal primase functions as a nanoscale caliper to define primer length.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. 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

5 authors at 2 institutions in 2 countries.

Sandro HolzerDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, UK.
Jiangyu YanMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, 47405, USA.
Mairi L KilkennyDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, UK.
Stephen D BellMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, 47405, USA. stedbell@indiana.edu.ORCID http://orcid.org/0000-0002-8474-6592
Luca PellegriniDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, UK. lp212@cam.ac.uk.ORCID http://orcid.org/0000-0002-9300-497X
University of Cambridge · GBIndiana University Bloomington · US

Funding

Wellcome Trust 104641/Z/14/Z
6 · The paper itself

Abstract

DNA replication depends on primase, the specialised polymerase responsible for synthesis of the RNA primers that are elongated by the replicative DNA polymerases. In eukaryotic and archaeal replication, primase is a heterodimer of two subunits, PriS and PriL. Recently, a third primase subunit named PriX was identified in the archaeon Sulfolobus solfataricus. PriX is essential for primer synthesis and is structurally related to the Fe-S cluster domain of eukaryotic PriL. Here we show that PriX contains a nucleotide-binding site required for primer synthesis, and demonstrate equivalence of nucleotide-binding residues in PriX with eukaryotic PriL residues that are known to be important for primer synthesis. A primase chimera, where PriX is fused to a truncated version of PriL lacking the Fe-S cluster domain retains wild-type levels of primer synthesis. Our evidence shows that PriX has replaced PriL as the subunit that endows primase with the unique ability to initiate nucleic acid synthesis. Importantly, our findings reveal that the Fe-S cluster is not required for primer synthesis.

Identifiers

PMID29167441
PMCPMC5700102
OpenAlexW2768277772

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.