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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/85694

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network_name_str CONICET Digital (CONICET)
spelling 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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