Evidence map›Paper›PMID 26012696›Full record

ArticleCellular and molecular life sciences : CMLS2015

Two independently folding units of Plasmodium profilin suggest evolution via gene fusion.

Saligram Prabhakar Bhargav, Juha Vahokoski, Juha Pekka Kallio, Andrew E Torda, Petri Kursula, Inari Kursula

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Profilin1 biology and its mutation, actin(g) in disease.Cellular and molecular life sciences : CMLS · 2017
    Review
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 4 institutions in 3 countries.

Saligram Prabhakar BhargavFaculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland.
Juha VahokoskiFaculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland.
Juha Pekka KallioHelmholtz Centre for Infection Research, Notkestrasse 85, 22607, Hamburg, Germany.
Andrew E TordaCentre for Bioinformatics, University of Hamburg, Bundesstrasse 43, 20146, Hamburg, Germany.
Petri KursulaFaculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland.
Inari KursulaFaculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland. inari.kursula@oulu.fi.
University of Oulu · FIHelmholtz Centre for Infection Research · DEUniversität Hamburg · DEUniversity of Bergen · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gene fusion is a common mechanism of protein evolution that has mainly been discussed in the context of multidomain or symmetric proteins. Less is known about fusion of ancestral genes to produce small single-domain proteins. Here, we show with a domain-swapped mutant Plasmodium profilin that this small, globular, apparently single-domain protein consists of two foldons. The separation of binding sites for different protein ligands in the two halves suggests evolution via an ancient gene fusion event, analogous to the formation of multidomain proteins. Finally, the two fragments can be assembled together after expression as two separate gene products. The possibility to engineer both domain-swapped dimers and half-profilins that can be assembled back to a full profilin provides perspectives for engineering of novel protein folds, e.g., with different scaffolding functions.

Indexed as

Evolution, MolecularGene FusionCircular DichroismCrystallography, X-RayExonsIntronsModels, MolecularMutationPlasmodium falciparumProfilinsProtein FoldingProtein MultimerizationProtein SubunitsProtozoan ProteinsScattering, Small AngleX-Ray DiffractionProfilinsProtein SubunitsProtozoan ProteinsActin-binding proteinCrystal structureModularProtein interactionSequence analysisSmall-angle X-ray scatteringβ-Hairpin

Identifiers

PMID26012696
PMCPMC11113795
OpenAlexW1962668675

What OpenQuestion holds

Textmetadata
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.