Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins
- Autores
- Bustos, Diego Martin; Iglesias, Alberto Alvaro
- Año de publicación
- 2003
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Glyceraldehyde-3-phosphate dehydrogenases catalyze key steps in energy and reducing power partitioning in cells of higher plants. Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) present in heterotrophic cells of wheat (Triticum aestivum) was activated up to 3-fold by MgCl2. The effect was not observed with the non-phosphorylated enzyme found in leaves. The divalent cation also affected the response of the enzyme from endosperm and shoots to adenine nucleotides and inorganic pyrophosphate. Gel filtration chromatography, co-immunoprecipitation followed by immunostaining, and the use of a phosphopeptide containing a canonical binding motif showed that MgCl2 actually disrupted the interaction between GAPN and a 14-3-3 regulatory protein. After interaction with 14-3-3, phosphorylated GAPN exhibits a 3-fold lower Vmax and higher sensitivity to inhibition by ATP and pyrophosphate. Results suggest that GAPN is a target for regulation by phosphorylation, levels of divalent cations, and 14-3-3 proteins. The regulatory mechanism could be critical to maintain levels of energy and reductants in the cytoplasm of heterotrophic plant cells.
Fil: Bustos, Diego Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina - Materia
-
14-3-3 proteins
Precursor proteins
Subunit structure
Plant glycolysis - 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:11336/85694
Ver los metadatos del registro completo
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Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 ProteinsBustos, Diego MartinIglesias, Alberto Alvaro14-3-3 proteinsPrecursor proteinsSubunit structurePlant glycolysishttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Glyceraldehyde-3-phosphate dehydrogenases catalyze key steps in energy and reducing power partitioning in cells of higher plants. Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) present in heterotrophic cells of wheat (Triticum aestivum) was activated up to 3-fold by MgCl2. The effect was not observed with the non-phosphorylated enzyme found in leaves. The divalent cation also affected the response of the enzyme from endosperm and shoots to adenine nucleotides and inorganic pyrophosphate. Gel filtration chromatography, co-immunoprecipitation followed by immunostaining, and the use of a phosphopeptide containing a canonical binding motif showed that MgCl2 actually disrupted the interaction between GAPN and a 14-3-3 regulatory protein. After interaction with 14-3-3, phosphorylated GAPN exhibits a 3-fold lower Vmax and higher sensitivity to inhibition by ATP and pyrophosphate. Results suggest that GAPN is a target for regulation by phosphorylation, levels of divalent cations, and 14-3-3 proteins. The regulatory mechanism could be critical to maintain levels of energy and reductants in the cytoplasm of heterotrophic plant cells.Fil: Bustos, Diego Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaAmerican Society of Plant Biologist2003-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/85694Bustos, Diego Martin; Iglesias, Alberto Alvaro; Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins; American Society of Plant Biologist; Plant Physiology; 133; 4; 12-2003; 2081-20880032-0889CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1104/pp.103.030981info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:53:53Zoai:ri.conicet.gov.ar:11336/85694instacron: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 14:53:54.262CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins |
title |
Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins |
spellingShingle |
Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins Bustos, Diego Martin 14-3-3 proteins Precursor proteins Subunit structure Plant glycolysis |
title_short |
Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins |
title_full |
Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins |
title_fullStr |
Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins |
title_full_unstemmed |
Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins |
title_sort |
Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins |
dc.creator.none.fl_str_mv |
Bustos, Diego Martin Iglesias, Alberto Alvaro |
author |
Bustos, Diego Martin |
author_facet |
Bustos, Diego Martin Iglesias, Alberto Alvaro |
author_role |
author |
author2 |
Iglesias, Alberto Alvaro |
author2_role |
author |
dc.subject.none.fl_str_mv |
14-3-3 proteins Precursor proteins Subunit structure Plant glycolysis |
topic |
14-3-3 proteins Precursor proteins Subunit structure Plant glycolysis |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Glyceraldehyde-3-phosphate dehydrogenases catalyze key steps in energy and reducing power partitioning in cells of higher plants. Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) present in heterotrophic cells of wheat (Triticum aestivum) was activated up to 3-fold by MgCl2. The effect was not observed with the non-phosphorylated enzyme found in leaves. The divalent cation also affected the response of the enzyme from endosperm and shoots to adenine nucleotides and inorganic pyrophosphate. Gel filtration chromatography, co-immunoprecipitation followed by immunostaining, and the use of a phosphopeptide containing a canonical binding motif showed that MgCl2 actually disrupted the interaction between GAPN and a 14-3-3 regulatory protein. After interaction with 14-3-3, phosphorylated GAPN exhibits a 3-fold lower Vmax and higher sensitivity to inhibition by ATP and pyrophosphate. Results suggest that GAPN is a target for regulation by phosphorylation, levels of divalent cations, and 14-3-3 proteins. The regulatory mechanism could be critical to maintain levels of energy and reductants in the cytoplasm of heterotrophic plant cells. Fil: Bustos, Diego Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina |
description |
Glyceraldehyde-3-phosphate dehydrogenases catalyze key steps in energy and reducing power partitioning in cells of higher plants. Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) present in heterotrophic cells of wheat (Triticum aestivum) was activated up to 3-fold by MgCl2. The effect was not observed with the non-phosphorylated enzyme found in leaves. The divalent cation also affected the response of the enzyme from endosperm and shoots to adenine nucleotides and inorganic pyrophosphate. Gel filtration chromatography, co-immunoprecipitation followed by immunostaining, and the use of a phosphopeptide containing a canonical binding motif showed that MgCl2 actually disrupted the interaction between GAPN and a 14-3-3 regulatory protein. After interaction with 14-3-3, phosphorylated GAPN exhibits a 3-fold lower Vmax and higher sensitivity to inhibition by ATP and pyrophosphate. Results suggest that GAPN is a target for regulation by phosphorylation, levels of divalent cations, and 14-3-3 proteins. The regulatory mechanism could be critical to maintain levels of energy and reductants in the cytoplasm of heterotrophic plant cells. |
publishDate |
2003 |
dc.date.none.fl_str_mv |
2003-12 |
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/11336/85694 Bustos, Diego Martin; Iglesias, Alberto Alvaro; Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins; American Society of Plant Biologist; Plant Physiology; 133; 4; 12-2003; 2081-2088 0032-0889 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/85694 |
identifier_str_mv |
Bustos, Diego Martin; Iglesias, Alberto Alvaro; Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins; American Society of Plant Biologist; Plant Physiology; 133; 4; 12-2003; 2081-2088 0032-0889 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1104/pp.103.030981 |
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 application/pdf |
dc.publisher.none.fl_str_mv |
American Society of Plant Biologist |
publisher.none.fl_str_mv |
American Society of Plant Biologist |
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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1846083070333026304 |
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13.22299 |