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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/1632
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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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1846083456462749696 |
score |
13.22299 |