Evidence map›Paper›PMID 27208221›Full record

ArticlePlant physiology2016

A Light Switch Based on Protein S-Nitrosylation Fine-Tunes Photosynthetic Light Harvesting in Chlamydomonas.

Hanna Berger, Marcello De Mia, Samuel Morisse, Christophe H Marchand, Stéphane D Lemaire, Lutz Wobbe, Olaf Kruse

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2016. 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
2.3field-weighted citation impact, top 12% 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, 34 citations in OpenAlex.

  1. Article
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  6. COPlant, cell & environment · 2021
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  10. Glutathionylation primes soluble glyceraldehyde-3-phosphate dehydrogenase for late collapse into insoluble aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
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  15. Interplay between COPhysiologia plantarum
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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

7 authors at 4 institutions in 2 countries.

Hanna BergerBielefeld University, Faculty of Biology, Center for Biotechnology (CeBiTec), 33615 Bielefeld, Germany (H.B., L.W., O.K.); andSorbonne Universités, UPMC University of Paris 6, Centre National de la Recherche Scientifique, UMR8226, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Institut de Biologie Physico-Chimique, 75005 Paris, France (M.D.M., S.M., C.H.M., S.D.L.).
Marcello De MiaBielefeld University, Faculty of Biology, Center for Biotechnology (CeBiTec), 33615 Bielefeld, Germany (H.B., L.W., O.K.); andSorbonne Universités, UPMC University of Paris 6, Centre National de la Recherche Scientifique, UMR8226, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Institut de Biologie Physico-Chimique, 75005 Paris, France (M.D.M., S.M., C.H.M., S.D.L.).
Samuel MorisseBielefeld University, Faculty of Biology, Center for Biotechnology (CeBiTec), 33615 Bielefeld, Germany (H.B., L.W., O.K.); andSorbonne Universités, UPMC University of Paris 6, Centre National de la Recherche Scientifique, UMR8226, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Institut de Biologie Physico-Chimique, 75005 Paris, France (M.D.M., S.M., C.H.M., S.D.L.).ORCID 0000-0002-9214-7792
Christophe H MarchandBielefeld University, Faculty of Biology, Center for Biotechnology (CeBiTec), 33615 Bielefeld, Germany (H.B., L.W., O.K.); andSorbonne Universités, UPMC University of Paris 6, Centre National de la Recherche Scientifique, UMR8226, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Institut de Biologie Physico-Chimique, 75005 Paris, France (M.D.M., S.M., C.H.M., S.D.L.).ORCID 0000-0002-0729-3841
Stéphane D LemaireBielefeld University, Faculty of Biology, Center for Biotechnology (CeBiTec), 33615 Bielefeld, Germany (H.B., L.W., O.K.); andSorbonne Universités, UPMC University of Paris 6, Centre National de la Recherche Scientifique, UMR8226, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Institut de Biologie Physico-Chimique, 75005 Paris, France (M.D.M., S.M., C.H.M., S.D.L.).
Lutz WobbeBielefeld University, Faculty of Biology, Center for Biotechnology (CeBiTec), 33615 Bielefeld, Germany (H.B., L.W., O.K.); andSorbonne Universités, UPMC University of Paris 6, Centre National de la Recherche Scientifique, UMR8226, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Institut de Biologie Physico-Chimique, 75005 Paris, France (M.D.M., S.M., C.H.M., S.D.L.).
Olaf KruseBielefeld University, Faculty of Biology, Center for Biotechnology (CeBiTec), 33615 Bielefeld, Germany (H.B., L.W., O.K.); andSorbonne Universités, UPMC University of Paris 6, Centre National de la Recherche Scientifique, UMR8226, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Institut de Biologie Physico-Chimique, 75005 Paris, France (M.D.M., S.M., C.H.M., S.D.L.) olaf.kruse@uni-bielefeld.de.
Bielefeld University · DESorbonne Université · FRInstitut de Biologie Physico-Chimique · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosynthetic eukaryotes are challenged by a fluctuating light supply, demanding for a modulated expression of nucleus-encoded light-harvesting proteins associated with photosystem II (LHCII) to adjust light-harvesting capacity to the prevailing light conditions. Here, we provide clear evidence for a regulatory circuit that controls cytosolic LHCII translation in response to light quantity changes. In the green unicellular alga Chlamydomonas reinhardtii, the cytosolic RNA-binding protein NAB1 represses translation of certain LHCII isoform mRNAs. Specific nitrosylation of Cys-226 decreases NAB1 activity and could be demonstrated in vitro and in vivo. The less active, nitrosylated form of NAB1 is found in cells acclimated to limiting light supply, which permits accumulation of light-harvesting proteins and efficient light capture. In contrast, elevated light supply causes its denitrosylation, thereby activating the repression of light-harvesting protein synthesis, which is needed to control excitation pressure at photosystem II. Denitrosylation of recombinant NAB1 is efficiently performed by the cytosolic thioredoxin system in vitro. To our knowledge, NAB1 is the first example of stimulus-induced denitrosylation in the context of photosynthetic acclimation. By identifying this novel redox cross-talk pathway between chloroplast and cytosol, we add a new key element required for drawing a precise blue print of the regulatory network of light harvesting.

Indexed as

Algal ProteinsCell NucleusChlamydomonasCysteineCytosolLightLight-Harvesting Protein ComplexesModels, MolecularOxidation-ReductionPhotosynthesisPhotosystem II Protein ComplexRNA-Binding ProteinsRNA, MessengerThioredoxinsThylakoidsAlgal ProteinsCysteineLight-Harvesting Protein ComplexesPhotosystem II Protein ComplexRNA-Binding ProteinsRNA, MessengerThioredoxins

Identifiers

PMID27208221
PMCPMC4902583
OpenAlexW2418071379

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.