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Cited by 314

The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.

The NADPH-dependent thioredoxin system constitutes a functional backup for cytosolic glutathione reductase in Arabidopsis

Open access
Marty, Laurent, Siala, Wafi, Schwarzländer, Markus, Fricker, Mark D., Wirtz, Markus, Sweetlove, Lee J., Meyer, Yves, Meyer, Andreas J., Reichheld, Jean-Philippe, Hell, Rüdiger·2009·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0900206106
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Abstract

Tight control of cellular redox homeostasis is essential for protection against oxidative damage and for maintenance of normal metabolism as well as redox signaling events. Under oxidative stress conditions, the tripeptide glutathione can switch from its reduced form (GSH) to oxidized glutathione disulfide (GSSG), and thus, forms an important cellular redox buffer. GSSG is normally reduced to GSH by 2 glutathione reductase (GR) isoforms encoded in the Arabidopsis genome, cytosolic GR1 and GR2 dual-targeted to chloroplasts and mitochondria. Measurements of total GR activity in leaf extracts of wild-type and 2 gr1 deletion mutants revealed that ≈65% of the total GR activity is attributed to GR1, whereas ≈35% is contributed by GR2. Despite the lack of a large share in total GR activity, gr1 mutants do not show any informative phenotype, even under stress conditions, and thus, the physiological impact of GR1 remains obscure. To elucidate its role in plants, glutathione-specific redox-sensitive GFP was used to dynamically measure the glutathione redox potential ( E GSH ) in the cytosol. Using this tool, it is shown that E GSH in gr1 mutants is significantly shifted toward more oxidizing conditions. Surprisingly, dynamic reduction of GSSG formed during induced oxidative stress in gr1 mutants is still possible, although significantly delayed compared with wild-type plants. We infer that there is functional redundancy in this critical pathway. Integrated biochemical and genetic assays identify the NADPH-dependent thioredoxin system as a backup system for GR1. Deletion of both, NADPH-dependent thioredoxin reductase A and GR1, prevents survival due to a pollen lethal phenotype.

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Metadata

Authors
Marty, L., Siala, W., Schwarzländer, M., Fricker, M. D., Wirtz, M., Sweetlove, L. J., Meyer, Y., Meyer, A. J., Reichheld, J.-P., & Hell, R.
Venue
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Published
2009-06-02
Volume
106
Issue
22
Pages
9109-9114
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.0900206106
OpenAlex
W1996039892
Cited by
314
References
42
FWCI
7.44
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: The NADPH-dependent thioredoxin system constitutes a functional backup for cytosolic glutathione reductase in Arabidopsis. https://app.cochat.ai/papers/10.1073/pnas.0900206106
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Marty, L., Siala, W., Schwarzländer, M., Fricker, M. D., Wirtz, M., Sweetlove, L. J., Meyer, Y., Meyer, A. J., Reichheld, J.-P., & Hell, R. (2009). The NADPH-dependent thioredoxin system constitutes a functional backup for cytosolic glutathione reductase in Arabidopsis. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0900206106

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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