Evidence map›Paper›PMID 21856338›Full record

ArticleMolecular and biochemical parasitology2011

The primase domain of PfPrex is a proteolytically matured, essential enzyme of the apicoplast.

Scott E Lindner, Manuel Llinás, James L Keck, Stefan H I Kappe

Abstract read
In one paragraph

Article in Molecular and biochemical parasitology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Apicoplast-Resident Processes: Exploiting the Chink in the Armour ofAdvances in pharmacological and pharmaceutical sciences · 2024
    Review
  7. Article
  8. Transient State Kinetics ofBiochemistry · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

4 authors at 3 institutions in 1 country.

Scott E LindnerDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, 550 Medical Sciences Center, 1300 University Avenue, Madison, WI 53706, USA. Scott.Lindner@SeattleBioMed.org
Manuel Llinás
James L Keck
Stefan H I Kappe
Center for Infectious Disease Research · USPrinceton University · USUniversity of Wisconsin–Madison · US

Funding

Structure and Function of Bacterial RecQ ProteinR01GM068061 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI KECK, JAMES L · 2003 to 2011
$2.7M
Structural Analysis of DNA Replication Machinery of P. falciparumF32GM083438 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI LINDNER, SCOTT E · 2009 to 2010
$102k
NIGMS NIH HHS F32 GM083438NIGMS NIH HHS F32GM083438NIGMS NIH HHS R01 GM068061
6 · The paper itself

Abstract

The apicoplast of Plasmodium is an essential organelle with its own circular genome that must be faithfully replicated and segregated to its progeny during parasite sporogony and schizogony. DNA replication proteins are not encoded by its genome. Instead, the replication machinery must be imported from nuclear-encoded genes. A likely apicoplast DNA replication factor, PfPrex, bears a bipartite leader sequence for apicoplast trafficking and contains several DNA replication-related enzymatic domains. Here we analyze the domain structure of PfPrex and examine its trafficking and maturation within the parasite. A minimal primase domain of PfPrex is shown to contain functional zinc-binding and TOPRIM-fold domains, which in a recombinant form are sufficient to produce RNA primers from a single-stranded DNA template. PfPrex is shown to be extensively proteolytically matured within the parasite, which effectively separates its functional domains. Gene targeting attempts to knockout the Plasmodium yoelii ortholog of Prex were unsuccessful, indicating the apparent essentiality of this protein to the parasite. Finally, overexpression in Plasmodium falciparum of PfPrex's trafficking and primase sequences yielded specific and dynamic localization to foci within the apicoplast. Taken together, these observations strongly suggest an essential role of PfPrex primase in the production of RNA primers for lagging strand DNA synthesis of the apicoplast genome.

Indexed as

AnimalsDNA PrimaseFemaleHumansMalaria, FalciparumMiceOrganellesPlasmodium falciparumProtein BindingProtein Structure, TertiaryProteolysisProtozoan ProteinsZincDNA PrimaseProtozoan ProteinsZinc

Identifiers

PMID21856338
PMCPMC3196721
OpenAlexW2024166392

What OpenQuestion holds

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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.