A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant Cells

Autores
Piattoni, Claudia Vanesa; Guerrero, Sergio Adrian; Iglesias, Alberto Alvaro
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Adaptation to aerobic life leads organisms to sense reactive oxygen species and use the signal for coordination of the entire metabolism. Glycolysis in plants is a particular network where specific steps, like oxidation of glyceraldehydes-3-phosphate (Ga3P), are critical in order for it to function. The triose-phosphate can be converted into 3-phosphoglycerate through the phosphorylating Ga3P dehydrogenase (Ga3PDHase, EC 1.2.1.12) producing ATP and NADH, or via the non-phosphorylating enzyme (np-Ga3PDHase; EC 1.2.1.9) generating NADPH. In this work we found redox regulation to be a posttranslational mechanism allowing the fine-tuning of the triose-phosphate fate. Both enzymes were inactivated after oxidation by reactive oxygen and nitrogen species. Kinetic studies determined that Ga3PDHase is marked (63-fold) more sensitive to oxidants than np-Ga3PDHase. Thioredoxin-h reverted the oxidation of both enzymes (although with differences between them), suggesting a physiological redox regulation. The results support a metabolic scenario where the cytosolic triose-phosphate dehydrogenases are regulated under changeable redox conditions. This would allow coordinate production of NADPH or ATP through glycolysis, with oxidative signals triggering reducing power synthesis in the cytosol. The NADPH increment would favor antioxidant responses to cope with the oxidative situation, while the thioredoxin system would positively feedback NADPH production by maintaining np-Ga3PDHase at its reduced active state.
Fil: Piattoni, Claudia Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
Fil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
Materia
Triose-phosphate
Glyceraldehyde-3-phosphate
Dehydrogenase
Reactive oxygen species
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/1632

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network_name_str CONICET Digital (CONICET)
spelling A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant CellsPiattoni, Claudia VanesaGuerrero, Sergio AdrianIglesias, Alberto AlvaroTriose-phosphateGlyceraldehyde-3-phosphateDehydrogenaseReactive oxygen specieshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Adaptation to aerobic life leads organisms to sense reactive oxygen species and use the signal for coordination of the entire metabolism. Glycolysis in plants is a particular network where specific steps, like oxidation of glyceraldehydes-3-phosphate (Ga3P), are critical in order for it to function. The triose-phosphate can be converted into 3-phosphoglycerate through the phosphorylating Ga3P dehydrogenase (Ga3PDHase, EC 1.2.1.12) producing ATP and NADH, or via the non-phosphorylating enzyme (np-Ga3PDHase; EC 1.2.1.9) generating NADPH. In this work we found redox regulation to be a posttranslational mechanism allowing the fine-tuning of the triose-phosphate fate. Both enzymes were inactivated after oxidation by reactive oxygen and nitrogen species. Kinetic studies determined that Ga3PDHase is marked (63-fold) more sensitive to oxidants than np-Ga3PDHase. Thioredoxin-h reverted the oxidation of both enzymes (although with differences between them), suggesting a physiological redox regulation. The results support a metabolic scenario where the cytosolic triose-phosphate dehydrogenases are regulated under changeable redox conditions. This would allow coordinate production of NADPH or ATP through glycolysis, with oxidative signals triggering reducing power synthesis in the cytosol. The NADPH increment would favor antioxidant responses to cope with the oxidative situation, while the thioredoxin system would positively feedback NADPH production by maintaining np-Ga3PDHase at its reduced active state.Fil: Piattoni, Claudia Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;Fil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;Molecular Diversity Preservation International2013-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/1632Piattoni, Claudia Vanesa; Guerrero, Sergio Adrian; Iglesias, Alberto Alvaro; A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant Cells; Molecular Diversity Preservation International; International Journal Of Molecular Sciences; 14; 4-2013; 8073-80921422-0067enginfo:eu-repo/semantics/altIdentifier/doi/10.3390/ijms14048073info:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1422-0067/14/4/8073info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:32:16Zoai:ri.conicet.gov.ar:11336/1632instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:32:16.945CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant Cells
title A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant Cells
spellingShingle A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant Cells
Piattoni, Claudia Vanesa
Triose-phosphate
Glyceraldehyde-3-phosphate
Dehydrogenase
Reactive oxygen species
title_short A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant Cells
title_full A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant Cells
title_fullStr A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant Cells
title_full_unstemmed A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant Cells
title_sort A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant Cells
dc.creator.none.fl_str_mv Piattoni, Claudia Vanesa
Guerrero, Sergio Adrian
Iglesias, Alberto Alvaro
author Piattoni, Claudia Vanesa
author_facet Piattoni, Claudia Vanesa
Guerrero, Sergio Adrian
Iglesias, Alberto Alvaro
author_role author
author2 Guerrero, Sergio Adrian
Iglesias, Alberto Alvaro
author2_role author
author
dc.subject.none.fl_str_mv Triose-phosphate
Glyceraldehyde-3-phosphate
Dehydrogenase
Reactive oxygen species
topic Triose-phosphate
Glyceraldehyde-3-phosphate
Dehydrogenase
Reactive oxygen species
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Adaptation to aerobic life leads organisms to sense reactive oxygen species and use the signal for coordination of the entire metabolism. Glycolysis in plants is a particular network where specific steps, like oxidation of glyceraldehydes-3-phosphate (Ga3P), are critical in order for it to function. The triose-phosphate can be converted into 3-phosphoglycerate through the phosphorylating Ga3P dehydrogenase (Ga3PDHase, EC 1.2.1.12) producing ATP and NADH, or via the non-phosphorylating enzyme (np-Ga3PDHase; EC 1.2.1.9) generating NADPH. In this work we found redox regulation to be a posttranslational mechanism allowing the fine-tuning of the triose-phosphate fate. Both enzymes were inactivated after oxidation by reactive oxygen and nitrogen species. Kinetic studies determined that Ga3PDHase is marked (63-fold) more sensitive to oxidants than np-Ga3PDHase. Thioredoxin-h reverted the oxidation of both enzymes (although with differences between them), suggesting a physiological redox regulation. The results support a metabolic scenario where the cytosolic triose-phosphate dehydrogenases are regulated under changeable redox conditions. This would allow coordinate production of NADPH or ATP through glycolysis, with oxidative signals triggering reducing power synthesis in the cytosol. The NADPH increment would favor antioxidant responses to cope with the oxidative situation, while the thioredoxin system would positively feedback NADPH production by maintaining np-Ga3PDHase at its reduced active state.
Fil: Piattoni, Claudia Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
Fil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
description Adaptation to aerobic life leads organisms to sense reactive oxygen species and use the signal for coordination of the entire metabolism. Glycolysis in plants is a particular network where specific steps, like oxidation of glyceraldehydes-3-phosphate (Ga3P), are critical in order for it to function. The triose-phosphate can be converted into 3-phosphoglycerate through the phosphorylating Ga3P dehydrogenase (Ga3PDHase, EC 1.2.1.12) producing ATP and NADH, or via the non-phosphorylating enzyme (np-Ga3PDHase; EC 1.2.1.9) generating NADPH. In this work we found redox regulation to be a posttranslational mechanism allowing the fine-tuning of the triose-phosphate fate. Both enzymes were inactivated after oxidation by reactive oxygen and nitrogen species. Kinetic studies determined that Ga3PDHase is marked (63-fold) more sensitive to oxidants than np-Ga3PDHase. Thioredoxin-h reverted the oxidation of both enzymes (although with differences between them), suggesting a physiological redox regulation. The results support a metabolic scenario where the cytosolic triose-phosphate dehydrogenases are regulated under changeable redox conditions. This would allow coordinate production of NADPH or ATP through glycolysis, with oxidative signals triggering reducing power synthesis in the cytosol. The NADPH increment would favor antioxidant responses to cope with the oxidative situation, while the thioredoxin system would positively feedback NADPH production by maintaining np-Ga3PDHase at its reduced active state.
publishDate 2013
dc.date.none.fl_str_mv 2013-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/1632
Piattoni, Claudia Vanesa; Guerrero, Sergio Adrian; Iglesias, Alberto Alvaro; A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant Cells; Molecular Diversity Preservation International; International Journal Of Molecular Sciences; 14; 4-2013; 8073-8092
1422-0067
url http://hdl.handle.net/11336/1632
identifier_str_mv Piattoni, Claudia Vanesa; Guerrero, Sergio Adrian; Iglesias, Alberto Alvaro; A Differential Redox Regulation or the Pathways Metabolizing Glyceraldehyde-3-phosphate Tunes the Production of Reducing Power in the Cytosol of Plant Cells; Molecular Diversity Preservation International; International Journal Of Molecular Sciences; 14; 4-2013; 8073-8092
1422-0067
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/ijms14048073
info:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1422-0067/14/4/8073
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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