Evidence map›Paper›PMID 33856472›Full record

ArticlePlant physiology2021

The function of glutaredoxin GRXS15 is required for lipoyl-dependent dehydrogenases in mitochondria.

Anna Moseler, Inga Kruse, Andrew E Maclean, Luca Pedroletti, Marina Franceschetti, Stephan Wagner, Regina Wehler, Katrin Fischer-Schrader, Gernot Poschet, Markus Wirtz and 6 more

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Plant physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Emerging roles of glutaredoxins in plant metabolism.Journal of experimental botany · 2026
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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

16 authors at 6 institutions in 3 countries.

Anna MoselerInstitute of Crop Science and Resource Conservation (INRES)-Chemical Signalling, University of Bonn, 53113 Bonn, Germany.ORCID 0000-0003-4641-8093
Inga KruseDepartment of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, UK.ORCID 0000-0003-1935-1647
Andrew E MacleanDepartment of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, UK.
Luca PedrolettiInstitute of Crop Science and Resource Conservation (INRES)-Chemical Signalling, University of Bonn, 53113 Bonn, Germany.ORCID 0000-0002-8594-1306
Marina FranceschettiDepartment of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, UK.ORCID 0000-0002-1389-6825
Stephan WagnerInstitute of Crop Science and Resource Conservation (INRES)-Chemical Signalling, University of Bonn, 53113 Bonn, Germany.ORCID 0000-0001-5369-7911
Regina WehlerInstitute of Molecular Physiology and Biotechnology of Plants (IMBIO), University of Bonn, 53115 Bonn, Germany.
Katrin Fischer-SchraderDepartment of Chemistry, Institute for Biochemistry, University of Cologne, 50674 Cologne, Germany.ORCID 0000-0003-4532-8918
Gernot PoschetCentre for Organismal Studies, University of Heidelberg, 69120 Heidelberg, Germany.
Markus WirtzCentre for Organismal Studies, University of Heidelberg, 69120 Heidelberg, Germany.ORCID 0000-0001-7790-4022
Peter DörmannInstitute of Molecular Physiology and Biotechnology of Plants (IMBIO), University of Bonn, 53115 Bonn, Germany.ORCID 0000-0002-5845-9370
Tatjana M HildebrandtInstitute of Plant Genetics, Leibniz University Hannover, 30167 Hannover, Germany.ORCID 0000-0002-3562-5241
Rüdiger HellCentre for Organismal Studies, University of Heidelberg, 69120 Heidelberg, Germany.ORCID 0000-0002-6238-4818
Markus SchwarzländerInstitute of Plant Biology and Biotechnology (IBBP)-Plant Energy Biology, University of Münster, 48143 Münster, Germany.
Janneke BalkDepartment of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, UK.ORCID 0000-0003-4738-1990
Andreas J MeyerInstitute of Crop Science and Resource Conservation (INRES)-Chemical Signalling, University of Bonn, 53113 Bonn, Germany.ORCID 0000-0001-8144-4364
University of Bonn · DEJohn Innes Centre · GBHeidelberg University · DELeibniz University Hannover · DEUniversity of Cologne · DEUniversity of Münster · DE

Funding

Biotechnology and Biological Sciences Research Council BB/P012523/1Biotechnology and Biological Sciences Research Council BB/P012574/1
6 · The paper itself

Abstract

Iron-sulfur (Fe-S) clusters are ubiquitous cofactors in all life and are used in a wide array of diverse biological processes, including electron transfer chains and several metabolic pathways. Biosynthesis machineries for Fe-S clusters exist in plastids, the cytosol, and mitochondria. A single monothiol glutaredoxin (GRX) is involved in Fe-S cluster assembly in mitochondria of yeast and mammals. In plants, the role of the mitochondrial homolog GRXS15 has only partially been characterized. Arabidopsis (Arabidopsis thaliana) grxs15 null mutants are not viable, but mutants complemented with the variant GRXS15 K83A develop with a dwarf phenotype similar to the knockdown line GRXS15amiR. In an in-depth metabolic analysis of the variant and knockdown GRXS15 lines, we show that most Fe-S cluster-dependent processes are not affected, including biotin biosynthesis, molybdenum cofactor biosynthesis, the electron transport chain, and aconitase in the tricarboxylic acid (TCA) cycle. Instead, we observed an increase in most TCA cycle intermediates and amino acids, especially pyruvate, glycine, and branched-chain amino acids (BCAAs). Additionally, we found an accumulation of branched-chain α-keto acids (BCKAs), the first degradation products resulting from transamination of BCAAs. In wild-type plants, pyruvate, glycine, and BCKAs are all metabolized through decarboxylation by mitochondrial lipoyl cofactor (LC)-dependent dehydrogenase complexes. These enzyme complexes are very abundant, comprising a major sink for LC. Because biosynthesis of LC depends on continuous Fe-S cluster supply to lipoyl synthase, this could explain why LC-dependent processes are most sensitive to restricted Fe-S supply in grxs15 mutants.

Indexed as

ArabidopsisDihydrolipoamide DehydrogenaseGenes, PlantGenetic VariationGenotypeGlutaredoxinsIron-Sulfur ProteinsMitochondriaDihydrolipoamide DehydrogenaseGlutaredoxinsIron-Sulfur Proteins

Identifiers

PMID33856472
PMCPMC8260144
OpenAlexW3152720756

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.