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Thioredoxins m regulate plastid glucose-6-phosphate dehydrogenase activity in Arabidopsis roots under salt stress
Plants contain several NADPH-producing enzymes including glucose-6-phosphate dehydrogenases (G6PDH) with different sub-cellular localizations. The activity of plastidial G6PDHs is redox-regulated by thioredoxins (TRX). Although specific TRXs are known to regulate chloroplastic isoforms of G6PDH, lit...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10274509/ https://www.ncbi.nlm.nih.gov/pubmed/37332692 http://dx.doi.org/10.3389/fpls.2023.1179112 |
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author | Née, Guillaume Wang, Fuzheng Châtel-Innocenti, Gilles Mhamdi, Amna Juranville, Eugénie Vanacker, Hélène Noctor, Graham Issakidis-Bourguet, Emmanuelle |
author_facet | Née, Guillaume Wang, Fuzheng Châtel-Innocenti, Gilles Mhamdi, Amna Juranville, Eugénie Vanacker, Hélène Noctor, Graham Issakidis-Bourguet, Emmanuelle |
author_sort | Née, Guillaume |
collection | PubMed |
description | Plants contain several NADPH-producing enzymes including glucose-6-phosphate dehydrogenases (G6PDH) with different sub-cellular localizations. The activity of plastidial G6PDHs is redox-regulated by thioredoxins (TRX). Although specific TRXs are known to regulate chloroplastic isoforms of G6PDH, little information is available for plastidic isoforms found in heterotrophic organs or tissues. Here, we investigated TRX regulation of the two G6PDH plastidic isoforms of Arabidopsis roots during exposure to a mild salt stress. We report that in vitro m-type TRXs are the most efficient regulators of the G6PDH2 and G6PDH3 mainly found in Arabidopsis roots. While expression of the corresponding G6PD and plastidic TRX genes was marginally affected by salt, it impaired root growth of several of the corresponding mutant lines. Using an in situ assay for G6PDH, G6PDH2 was found to be the major contributor to salt-induced increases in activity, while data from ROS assays further provide in vivo evidence that TRX m acts in redox regulation during salt stress. Taken together, our data suggest that regulation of plastid G6PDH activity by TRX m may be an important player regulating NADPH production in Arabidopsis roots undergoing salt stress. |
format | Online Article Text |
id | pubmed-10274509 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-102745092023-06-17 Thioredoxins m regulate plastid glucose-6-phosphate dehydrogenase activity in Arabidopsis roots under salt stress Née, Guillaume Wang, Fuzheng Châtel-Innocenti, Gilles Mhamdi, Amna Juranville, Eugénie Vanacker, Hélène Noctor, Graham Issakidis-Bourguet, Emmanuelle Front Plant Sci Plant Science Plants contain several NADPH-producing enzymes including glucose-6-phosphate dehydrogenases (G6PDH) with different sub-cellular localizations. The activity of plastidial G6PDHs is redox-regulated by thioredoxins (TRX). Although specific TRXs are known to regulate chloroplastic isoforms of G6PDH, little information is available for plastidic isoforms found in heterotrophic organs or tissues. Here, we investigated TRX regulation of the two G6PDH plastidic isoforms of Arabidopsis roots during exposure to a mild salt stress. We report that in vitro m-type TRXs are the most efficient regulators of the G6PDH2 and G6PDH3 mainly found in Arabidopsis roots. While expression of the corresponding G6PD and plastidic TRX genes was marginally affected by salt, it impaired root growth of several of the corresponding mutant lines. Using an in situ assay for G6PDH, G6PDH2 was found to be the major contributor to salt-induced increases in activity, while data from ROS assays further provide in vivo evidence that TRX m acts in redox regulation during salt stress. Taken together, our data suggest that regulation of plastid G6PDH activity by TRX m may be an important player regulating NADPH production in Arabidopsis roots undergoing salt stress. Frontiers Media S.A. 2023-06-02 /pmc/articles/PMC10274509/ /pubmed/37332692 http://dx.doi.org/10.3389/fpls.2023.1179112 Text en Copyright © 2023 Née, Wang, Châtel-Innocenti, Mhamdi, Juranville, Vanacker, Noctor and Issakidis-Bourguet https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Née, Guillaume Wang, Fuzheng Châtel-Innocenti, Gilles Mhamdi, Amna Juranville, Eugénie Vanacker, Hélène Noctor, Graham Issakidis-Bourguet, Emmanuelle Thioredoxins m regulate plastid glucose-6-phosphate dehydrogenase activity in Arabidopsis roots under salt stress |
title | Thioredoxins m regulate plastid glucose-6-phosphate dehydrogenase activity in Arabidopsis roots under salt stress |
title_full | Thioredoxins m regulate plastid glucose-6-phosphate dehydrogenase activity in Arabidopsis roots under salt stress |
title_fullStr | Thioredoxins m regulate plastid glucose-6-phosphate dehydrogenase activity in Arabidopsis roots under salt stress |
title_full_unstemmed | Thioredoxins m regulate plastid glucose-6-phosphate dehydrogenase activity in Arabidopsis roots under salt stress |
title_short | Thioredoxins m regulate plastid glucose-6-phosphate dehydrogenase activity in Arabidopsis roots under salt stress |
title_sort | thioredoxins m regulate plastid glucose-6-phosphate dehydrogenase activity in arabidopsis roots under salt stress |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10274509/ https://www.ncbi.nlm.nih.gov/pubmed/37332692 http://dx.doi.org/10.3389/fpls.2023.1179112 |
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