Evidence map›Paper›PMID 32245955›Full record

ArticleNature communications2020

Mild proteasomal stress improves photosynthetic performance in Arabidopsis chloroplasts.

Julia Grimmer, Stefan Helm, Dirk Dobritzsch, Gerd Hause, Gerta Shema, René P Zahedi, Sacha Baginsky

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. 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
1.9field-weighted citation impact, top 14% 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

7 authors at 4 institutions in 2 countries.

Julia GrimmerInstitute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Saale, Germany.
Stefan HelmInstitute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Saale, Germany.
Dirk DobritzschInstitute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Saale, Germany.
Gerd HauseBiocenter of the University, Martin-Luther-University Halle-Wittenberg, Weinbergweg 22, 06120, Halle, Saale, Germany.
Gerta ShemaLeibniz-Institut für Analytische Wissenschaften -ISAS- e.V., Bunsen-Kirchhoff-Straße 11, 44139, Dortmund, Germany.
René P ZahediLeibniz-Institut für Analytische Wissenschaften -ISAS- e.V., Bunsen-Kirchhoff-Straße 11, 44139, Dortmund, Germany.
Sacha BaginskyInstitute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Saale, Germany. sacha.baginsky@rub.de.ORCID http://orcid.org/0000-0002-5440-3898
Martin Luther University Halle-Wittenberg · DEJewish General Hospital · CALeibniz Institute for Analytical Sciences - ISAS · DEUniversity Hospitals of the Ruhr-University of Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proteasome is an essential protein-degradation machinery in eukaryotic cells that controls protein turnover and thereby the biogenesis and function of cell organelles. Chloroplasts import thousands of nuclear-encoded precursor proteins from the cytosol, suggesting that the bulk of plastid proteins is transiently exposed to the cytosolic proteasome complex. Therefore, there is a cytosolic equilibrium between chloroplast precursor protein import and proteasomal degradation. We show here that a shift in this equilibrium, induced by mild genetic proteasome impairment, results in elevated precursor protein abundance in the cytosol and significantly increased accumulation of functional photosynthetic complexes in protein import-deficient chloroplasts. Importantly, a proteasome lid mutant shows improved photosynthetic performance, even in the absence of an import defect, signifying that functional precursors are continuously degraded. Hence, turnover of plastid precursors in the cytosol represents a mechanism to constrain thylakoid membrane assembly and photosynthetic electron transport.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplast ProteinsChloroplastsCytosolMutationPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPlants, Genetically ModifiedProteasome Endopeptidase ComplexProtein PrecursorsProteolysisStress, PhysiologicalArabidopsis ProteinsChloroplast ProteinsPhotosynthetic Reaction Center Complex ProteinsProteasome Endopeptidase ComplexProtein Precursors

Identifiers

PMID32245955
PMCPMC7125294
OpenAlexW3014867075

What OpenQuestion holds

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LicenceCC BY
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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.