The Functional Relationship between NADPH Thioredoxin Reductase C, 2-Cys Peroxiredoxins, and m-Type Thioredoxins in the Regulation of Calvin–Benson Cycle and Malate-Valve Enzymes in Arabidopsis

The concerted regulation of chloroplast biosynthetic pathways and NADPH extrusion via malate valve depends on f and m thioredoxins (Trxs). The finding that decreased levels of the thiol-peroxidase 2-Cys peroxiredoxin (Prx) suppress the severe phenotype of Arabidopsis mutants lacking NADPH-dependent...

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Autores: Delgado Requerey, Víctor, Cejudo Fernández, Francisco Javier, González García, María de la Cruz
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Recursos:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/155673
Acesso em linha:https://hdl.handle.net/11441/155673
https://doi.org/10.3390/antiox12051041
Access Level:acceso abierto
Palavra-chave:2-Cys peroxiredoxin
Calvin–Benson cycle
Chloroplast
Malate valve
NADPH-dependent Trx reductase (NTRC)
Redox regulation
Thioredoxin
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spelling The Functional Relationship between NADPH Thioredoxin Reductase C, 2-Cys Peroxiredoxins, and m-Type Thioredoxins in the Regulation of Calvin–Benson Cycle and Malate-Valve Enzymes in ArabidopsisDelgado Requerey, VíctorCejudo Fernández, Francisco JavierGonzález García, María de la Cruz2-Cys peroxiredoxinCalvin–Benson cycleChloroplastMalate valveNADPH-dependent Trx reductase (NTRC)Redox regulationThioredoxinThe concerted regulation of chloroplast biosynthetic pathways and NADPH extrusion via malate valve depends on f and m thioredoxins (Trxs). The finding that decreased levels of the thiol-peroxidase 2-Cys peroxiredoxin (Prx) suppress the severe phenotype of Arabidopsis mutants lacking NADPH-dependent Trx reductase C (NTRC) and Trxs f uncovered the central function of the NTRC-2-Cys-Prx redox system in chloroplast performance. These results suggest that Trxs m are also regulated by this system; however, the functional relationship between NTRC, 2-Cys Prxs, and m-type Trxs is unknown. To address this issue, we generated Arabidopsis thaliana mutants combining deficiencies in NTRC, 2-Cys Prx B, Trxs m1, and m4. The single trxm1 and trxm4 mutants showed a wild-type phenotype, growth retardation being noticed only in the trxm1m4 double mutant. Moreover, the ntrc-trxm1m4 mutant displayed a more severe phenotype than the ntrc mutant, as shown by the impaired photosynthetic performance, altered chloroplast structure, and defective light-dependent reduction in the Calvin–Benson cycle and malate-valve enzymes. These effects were suppressed by the decreased contents of 2-Cys Prx, since the quadruple ntrc-trxm1m4-2cpb mutant displayed a wild-type-like phenotype. These results show that the activity of m-type Trxs in the light-dependent regulation of biosynthetic enzymes and malate valve is controlled by the NTRC-2-Cys-Prx system.Ministerio de Ciencia e Innovación PID2020-115156GB-100Junta de Andalucía P20_00567Multidisciplinary Digital Publishing Institute (MDPI)Bioquímica Vegetal y Biología MolecularMinisterio de Ciencia e Innovación (MICIN). EspañaJunta de Andalucía2023info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/155673https://doi.org/10.3390/antiox12051041reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésAntioxidants, 12 (5), 1041.PID2020-115156GB-100P20_00567https://doi.org/10.3390/antiox12051041info:eu-repo/semantics/openAccessoai:idus.us.es:11441/1556732026-06-17T12:51:07Z
dc.title.none.fl_str_mv The Functional Relationship between NADPH Thioredoxin Reductase C, 2-Cys Peroxiredoxins, and m-Type Thioredoxins in the Regulation of Calvin–Benson Cycle and Malate-Valve Enzymes in Arabidopsis
title The Functional Relationship between NADPH Thioredoxin Reductase C, 2-Cys Peroxiredoxins, and m-Type Thioredoxins in the Regulation of Calvin–Benson Cycle and Malate-Valve Enzymes in Arabidopsis
spellingShingle The Functional Relationship between NADPH Thioredoxin Reductase C, 2-Cys Peroxiredoxins, and m-Type Thioredoxins in the Regulation of Calvin–Benson Cycle and Malate-Valve Enzymes in Arabidopsis
Delgado Requerey, Víctor
2-Cys peroxiredoxin
Calvin–Benson cycle
Chloroplast
Malate valve
NADPH-dependent Trx reductase (NTRC)
Redox regulation
Thioredoxin
title_short The Functional Relationship between NADPH Thioredoxin Reductase C, 2-Cys Peroxiredoxins, and m-Type Thioredoxins in the Regulation of Calvin–Benson Cycle and Malate-Valve Enzymes in Arabidopsis
title_full The Functional Relationship between NADPH Thioredoxin Reductase C, 2-Cys Peroxiredoxins, and m-Type Thioredoxins in the Regulation of Calvin–Benson Cycle and Malate-Valve Enzymes in Arabidopsis
title_fullStr The Functional Relationship between NADPH Thioredoxin Reductase C, 2-Cys Peroxiredoxins, and m-Type Thioredoxins in the Regulation of Calvin–Benson Cycle and Malate-Valve Enzymes in Arabidopsis
title_full_unstemmed The Functional Relationship between NADPH Thioredoxin Reductase C, 2-Cys Peroxiredoxins, and m-Type Thioredoxins in the Regulation of Calvin–Benson Cycle and Malate-Valve Enzymes in Arabidopsis
title_sort The Functional Relationship between NADPH Thioredoxin Reductase C, 2-Cys Peroxiredoxins, and m-Type Thioredoxins in the Regulation of Calvin–Benson Cycle and Malate-Valve Enzymes in Arabidopsis
dc.creator.none.fl_str_mv Delgado Requerey, Víctor
Cejudo Fernández, Francisco Javier
González García, María de la Cruz
author Delgado Requerey, Víctor
author_facet Delgado Requerey, Víctor
Cejudo Fernández, Francisco Javier
González García, María de la Cruz
author_role author
author2 Cejudo Fernández, Francisco Javier
González García, María de la Cruz
author2_role author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
Ministerio de Ciencia e Innovación (MICIN). España
Junta de Andalucía
dc.subject.none.fl_str_mv 2-Cys peroxiredoxin
Calvin–Benson cycle
Chloroplast
Malate valve
NADPH-dependent Trx reductase (NTRC)
Redox regulation
Thioredoxin
topic 2-Cys peroxiredoxin
Calvin–Benson cycle
Chloroplast
Malate valve
NADPH-dependent Trx reductase (NTRC)
Redox regulation
Thioredoxin
description The concerted regulation of chloroplast biosynthetic pathways and NADPH extrusion via malate valve depends on f and m thioredoxins (Trxs). The finding that decreased levels of the thiol-peroxidase 2-Cys peroxiredoxin (Prx) suppress the severe phenotype of Arabidopsis mutants lacking NADPH-dependent Trx reductase C (NTRC) and Trxs f uncovered the central function of the NTRC-2-Cys-Prx redox system in chloroplast performance. These results suggest that Trxs m are also regulated by this system; however, the functional relationship between NTRC, 2-Cys Prxs, and m-type Trxs is unknown. To address this issue, we generated Arabidopsis thaliana mutants combining deficiencies in NTRC, 2-Cys Prx B, Trxs m1, and m4. The single trxm1 and trxm4 mutants showed a wild-type phenotype, growth retardation being noticed only in the trxm1m4 double mutant. Moreover, the ntrc-trxm1m4 mutant displayed a more severe phenotype than the ntrc mutant, as shown by the impaired photosynthetic performance, altered chloroplast structure, and defective light-dependent reduction in the Calvin–Benson cycle and malate-valve enzymes. These effects were suppressed by the decreased contents of 2-Cys Prx, since the quadruple ntrc-trxm1m4-2cpb mutant displayed a wild-type-like phenotype. These results show that the activity of m-type Trxs in the light-dependent regulation of biosynthetic enzymes and malate valve is controlled by the NTRC-2-Cys-Prx system.
publishDate 2023
dc.date.none.fl_str_mv 2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/155673
https://doi.org/10.3390/antiox12051041
url https://hdl.handle.net/11441/155673
https://doi.org/10.3390/antiox12051041
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Antioxidants, 12 (5), 1041.
PID2020-115156GB-100
P20_00567
https://doi.org/10.3390/antiox12051041
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute (MDPI)
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute (MDPI)
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,198674

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