Evidence map›Paper›PMID 26147209›Full record

ArticlePloS one2015

Phytoene Desaturase from Oryza sativa: Oligomeric Assembly, Membrane Association and Preliminary 3D-Analysis.

Sandra Gemmecker, Patrick Schaub, Julian Koschmieder, Anton Brausemann, Friedel Drepper, Marta Rodriguez-Franco, Sandro Ghisla, Bettina Warscheid, Oliver Einsle, Peter Beyer

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

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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

10 authors at 2 institutions in 1 country.

Sandra GemmeckerFaculty of Biology, Cell Biology, University of Freiburg, Freiburg, Germany.
Patrick SchaubFaculty of Biology, Cell Biology, University of Freiburg, Freiburg, Germany.
Julian KoschmiederFaculty of Biology, Cell Biology, University of Freiburg, Freiburg, Germany.
Anton BrausemannFaculty of Chemistry and Pharmacy, Institute for Biochemistry, University of Freiburg, Freiburg, Germany.
Friedel DrepperFaculty of Biology, Biochemistry and Functional Proteomics, University of Freiburg, Freiburg, Germany.
Marta Rodriguez-FrancoFaculty of Biology, Cell Biology, University of Freiburg, Freiburg, Germany.
Sandro GhislaDepartment of Biology, University of Konstanz, Konstanz, Germany.
Bettina WarscheidFaculty of Biology, Biochemistry and Functional Proteomics, University of Freiburg, Freiburg, Germany; BIOSS Centre for Biological Signalling Studies, University of Freiburg, Freiburg, Germany.
Oliver EinsleFaculty of Chemistry and Pharmacy, Institute for Biochemistry, University of Freiburg, Freiburg, Germany; BIOSS Centre for Biological Signalling Studies, University of Freiburg, Freiburg, Germany.
Peter BeyerFaculty of Biology, Cell Biology, University of Freiburg, Freiburg, Germany.
University of Freiburg · DEUniversity of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recombinant phytoene desaturase (PDS-His6) from rice was purified to near-homogeneity and shown to be enzymatically active in a biphasic, liposome-based assay system. The protein contains FAD as the sole protein-bound redox-cofactor. Benzoquinones, not replaceable by molecular oxygen, serve as a final electron acceptor defining PDS as a 15-cis-phytoene (donor):plastoquinone oxidoreductase. The herbicidal PDS-inhibitor norflurazon is capable of arresting the reaction by stabilizing the intermediary FAD(red), while an excess of the quinone acceptor relieves this blockage, indicating competition. The enzyme requires its homo-oligomeric association for activity. The sum of data collected through gel permeation chromatography, non-denaturing polyacrylamide electrophoresis, chemical cross-linking, mass spectrometry and electron microscopy techniques indicate that the high-order oligomers formed in solution are the basis for an active preparation. Of these, a tetramer consisting of dimers represents the active unit. This is corroborated by our preliminary X-ray structural analysis that also revealed similarities of the protein fold with the sequence-inhomologous bacterial phytoene desaturase CRTI and other oxidoreductases of the GR2-family of flavoproteins. This points to an evolutionary relatedness of CRTI and PDS yielding different carotene desaturation sequences based on homologous protein folds.

Indexed as

BiopolymersCell MembraneCrystallography, X-RayMass SpectrometryMicroscopy, Electron, ScanningNative Polyacrylamide Gel ElectrophoresisOryzaOxidoreductasesProtein BindingProtein ConformationBiopolymersOxidoreductasesphytoene dehydrogenase

Identifiers

PMID26147209
PMCPMC4492965
OpenAlexW2340775888

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.