Evidence map›Paper›PMID 33685582›Full record

ArticleeLife2021

Regulation of photosynthetic electron flow on dark to light transition by ferredoxin:NADP(H) oxidoreductase interactions.

Manuela Kramer, Melvin Rodriguez-Heredia, Francesco Saccon, Laura Mosebach, Manuel Twachtmann, Anja Krieger-Liszkay, Chris Duffy, Robert J Knell, Giovanni Finazzi, Guy Thomas Hanke

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. 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, 33 citations in OpenAlex.

  1. Structural proteomics reveals the functional docking interface of ferredoxin-NADPThe Plant journal : for cell and molecular biology · 2026
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  8. STN7 is not essential for developmental acclimation of Arabidopsis to light intensity.The Plant journal : for cell and molecular biology · 2023
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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 4 institutions in 3 countries.

Manuela KramerSchool of Biochemistry and Chemistry, Queen Mary University of London, London, United Kingdom.
Melvin Rodriguez-HerediaSchool of Biochemistry and Chemistry, Queen Mary University of London, London, United Kingdom.
Francesco SacconSchool of Biochemistry and Chemistry, Queen Mary University of London, London, United Kingdom.
Laura MosebachInstitute of Plant Biology and Biotechnology, University of Münster, Münster, Germany.
Manuel TwachtmannDepartment of Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, Osnabrück, Germany.
Anja Krieger-LiszkayInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay, Paris, France.
Chris DuffySchool of Biochemistry and Chemistry, Queen Mary University of London, London, United Kingdom.
Robert J KnellSchool of Biochemistry and Chemistry, Queen Mary University of London, London, United Kingdom.ORCID 0000-0002-3446-8715
Giovanni FinazziLaboratoire de Physiologie Cellulaire et Végétale, UMR 5168, Centre National de la Recherche Scientifique (CNRS), Commissariat a` l'Energie Atomique et aux Energies Alternatives (CEA), Université Grenoble Alpes, Institut National Recherche Agronomique (INRA), Institut de Recherche en Sciences et Technologies pour le Vivant (iRTSV), CEA Grenoble, Grenoble, France.
Guy Thomas HankeSchool of Biochemistry and Chemistry, Queen Mary University of London, London, United Kingdom.ORCID 0000-0002-6167-926X
Queen Mary University of London · GBCentre National de la Recherche Scientifique · FROsnabrück University · DEUniversity of Münster · DE

Funding

Biotechnology and Biological Sciences Research Council BB/R004838/1
6 · The paper itself

Abstract

During photosynthesis, electron transport is necessary for carbon assimilation and must be regulated to minimize free radical damage. There is a longstanding controversy over the role of a critical enzyme in this process (ferredoxin:NADP(H) oxidoreductase, or FNR), and in particular its location within chloroplasts. Here we use immunogold labelling to prove that FNR previously assigned as soluble is in fact membrane associated. We combined this technique with a genetic approach in the model plant Arabidopsis to show that the distribution of this enzyme between different membrane regions depends on its interaction with specific tether proteins. We further demonstrate a correlation between the interaction of FNR with different proteins and the activity of alternative photosynthetic electron transport pathways. This supports a role for FNR location in regulating photosynthetic electron flow during the transition from dark to light.

Indexed as

ElectronsPhotosynthesisArabidopsisArabidopsis ProteinsBiological TransportChloroplastsFerredoxin-NADP ReductasePhotoperiodArabidopsis ProteinsFerredoxin-NADP ReductaseFNR1 protein, ArabidopsisA. thalianachloroplastelectron transportferredoxinNADPHphotosynthesisplant biologythylakoid

Identifiers

PMID33685582
PMCPMC7984839
OpenAlexW3134457645

What OpenQuestion holds

Textmetadata
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.