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  Thioredoxin h2 contributes to the redox regulation of mitochondrial photorespiratory metabolism

da Fonseca-Pereira, P., Souza, P. V., Hou, L.-Y., Schwab, S., Geigenberger, P., Nunes-Nesi, A., et al. (2020). Thioredoxin h2 contributes to the redox regulation of mitochondrial photorespiratory metabolism. Plant, Cell and Environment, 43(1), 188-208. doi:10.1111/pce.13640.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-3F2A-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-6CA0-D
Genre: Journal Article

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 Creators:
da Fonseca-Pereira, Paula1, Author
Souza, Paulo V.L.1, Author
Hou, Liang-Yu1, Author
Schwab, Saskia1, Author
Geigenberger, Peter1, Author
Nunes-Nesi, Adriano1, Author
Timm, Stefan1, Author
Fernie, A. R.2, Author              
Thormählen, Ina1, Author
Araújo, Wagner L.1, Author
Daloso, Danilo M.1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Central Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753339              

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Free keywords: Glycine decarboxylase, mitochondria, mitochondrial lipoamide dehydrogenase, photorespiration, redox regulation, thioredoxin
 Abstract: Abstract Thioredoxins (TRX) are important proteins involved in redox regulation of metabolism. In plants, it has been shown that the mitochondrial metabolism is regulated by the mitochondrial TRX system. However, the functional significance of TRX h2, which is found at both cytosol and mitochondria, remains unclear. Arabidopsis plants lacking TRX h2 showed delayed seed germination and reduced respiration alongside impaired stomatal and mesophyll conductance, without impacting photosynthesis under ambient O2 conditions. However, an increase in the stoichiometry of photorespiratory CO2 release was found during O2-dependent gas exchange measurements in trxh2 mutants. Metabolite profiling of trxh2 leaves revealed alterations in key metabolites of photorespiration and in several metabolites involved in respiration and amino acid metabolism. Decreased abundance of serine hydroxymethyltransferase and glycine decarboxylase (GDC) H and L subunits as well as reduced NADH/NAD+ ratios were also observed in trxh2 mutants. We further demonstrated that the redox status of GDC-L is altered in trxh2 mutants in vivo and that recombinant TRX h2 can deactivate GDC-L in vitro, indicating that this protein is redox regulated by the TRX system. Collectively, our results demonstrate that TRX h2 plays an important role in the redox regulation of mitochondrial photorespiratory metabolism.

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Language(s): eng - English
 Dates: 201920192020
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1111/pce.13640
BibTex Citekey: doi:10.1111/pce.13640
 Degree: -

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Title: Plant, Cell and Environment
  Other : Plant, Cell & Environment
Source Genre: Journal
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Publ. Info: Oxford, England : Blackwell Science
Pages: - Volume / Issue: 43 (1) Sequence Number: - Start / End Page: 188 - 208 Identifier: ISSN: 0140-7791
CoNE: https://pure.mpg.de/cone/journals/resource/954925471334