A complex and dynamic redox network regulates oxygen reduction at photosystem I in Arabidopsis.


Journal

Plant physiology
ISSN: 1532-2548
Titre abrégé: Plant Physiol
Pays: United States
ID NLM: 0401224

Informations de publication

Date de publication:
26 Sep 2024
Historique:
received: 10 05 2024
revised: 24 06 2024
accepted: 25 09 2024
medline: 26 9 2024
pubmed: 26 9 2024
entrez: 26 9 2024
Statut: aheadofprint

Résumé

Thiol-dependent redox regulation of enzyme activities plays a central role in regulating photosynthesis. Beside the regulation of metabolic pathways, alternative electron transport is subjected to thiol-dependent regulation. We investigated the regulation of O2 reduction at photosystem I. The level of O2 reduction in leaves and isolated thylakoid membranes depends on the photoperiod in which plants are grown. We used a set of Arabidopsis (Arabidopsis thaliana) mutant plants affected in the stromal, membrane and lumenal thiol network to study the redox protein partners involved in regulating O2 reduction. Light-dependent O2 reduction was determined in leaves and in thylakoids of plants grown in short day and long day conditions using a spin-trapping electron paramagnetic resonance (EPR) assay. In wild type samples from short day conditions, reactive oxygen species (ROS) generation was double that of samples from long day conditions, while this difference was abolished in several redoxin mutants. An in vitro reconstitution assay showed that thioredoxin m, NADPH-dependent reductase C and NADPH are required for high O2 reduction levels in thylakoids from plants grown in long day conditions. Using isolated photosystem I, we also showed that reduction of a photosystem I protein is responsible for the increase in O2 reduction. Furthermore, differences in the membrane localization of m-type thioredoxins and 2-Cys peroxiredoxin were detected between thylakoids of short day and long day plants. Overall, we propose a model of redox regulation of O2 reduction according to the reduction power of the stroma and the ability of different thiol-containing proteins to form a network of redox interactions.

Identifiants

pubmed: 39324622
pii: 7776034
doi: 10.1093/plphys/kiae501
pii:
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

© The Author(s) 2024. Published by Oxford University Press on behalf of American Society of Plant Biologists. All rights reserved. For commercial re-use, please contact reprints@oup.com for reprints and translation rights for reprints. All other permissions can be obtained through our RightsLink service via the Permissions link on the article page on our site—for further information please contact journals.permissions@oup.com.

Auteurs

Umama Hani (U)

Université Paris-Saclay, Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, 91198 Gif-sur-Yvette, France.

Belen Naranjo (B)

Instituto de Bioquímica Vegetal y Fotosíntesis, Departamento de Bioquímica Vegetal y Biología Molecular, Universidad de Sevilla, 41092 Sevilla, Spain.

Ginga Shimakawa (G)

Université Paris-Saclay, Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, 91198 Gif-sur-Yvette, France.

Christophe Espinasse (C)

Université Paris-Saclay, CNRS, INRAE, Université Evry, Institute of Plant Sciences Paris-Saclay (IPS2), 91190, Gif-sur-Yvette, France.

Hélène Vanacker (H)

Université Paris-Saclay, CNRS, INRAE, Université Evry, Institute of Plant Sciences Paris-Saclay (IPS2), 91190, Gif-sur-Yvette, France.

Pierre Sétif (P)

Université Paris-Saclay, Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, 91198 Gif-sur-Yvette, France.

Eevi Rintamäki (E)

Molecular Plant Biology, Department of Life Technologies, University of Turku, 20014 Turku, Finland.

Emmanuelle Issakidis-Bourguet (E)

Université Paris-Saclay, CNRS, INRAE, Université Evry, Institute of Plant Sciences Paris-Saclay (IPS2), 91190, Gif-sur-Yvette, France.

Anja Krieger-Liszkay (A)

Université Paris-Saclay, Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, 91198 Gif-sur-Yvette, France.

Classifications MeSH