Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoforms

Autores
Saigo, Mariana; Alvarez, Clarisa Ester; Andreo, Carlos Santiago; Drincovich, Maria Fabiana
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Malic enzyme is present in many plant cell compartments such as plastids, cytosol and mitochondria. Particularly relevant is the plastidial isoform that participates in the C4 cycle providing CO2 to RuBisCO in C4 species. This type of photosynthesis is more frequent among grasses where anatomical preconditioning would have facilitated the evolution of the C4 syndrome. In maize (C4 grass), the photosynthetic NADP dependent Malic enzyme (ZmC4-NADP-ME, L-malate:NADP oxidoreductase, E.C. 1.1.1.40) and the closest related non-photosynthetic isoform (ZmnonC4-NADPME, L-malate:NADP oxidoreductase, E.C. 1.1.1.40) are both plastidial but differ in expression pattern,kinetics and structure. Features like high catalytic efficiency, inhibition by high malate concentration at pH 7.0, redox modulation and tetramerization are characteristic of the photosynthetic NADP-ME. In this work, the proteins encoded by sorghum (C4 grass) and rice (C3 grass) NADP-ME genes,orthologues of the plastidial NADP-MEs from maize, were recombinantly expressed, purified and characterized. In a global comparison, we could identify a small group of residues which may explain the special features of C4 enzymes. Overall, the present work presents biochemical and molecular data that helps to elucidate the changes that took place in the evolution of C4 NADP-ME in grasses.
Fil: Saigo, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
Fil: Alvarez, Clarisa Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
Fil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
Fil: Drincovich, Maria Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
Materia
C4 Photosynthesis
Nadp-Malic Enzyme
Structure And Function Relasionship
Maize Sorghum Rice
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/3418

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network_name_str CONICET Digital (CONICET)
spelling Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoformsSaigo, MarianaAlvarez, Clarisa EsterAndreo, Carlos SantiagoDrincovich, Maria FabianaC4 PhotosynthesisNadp-Malic EnzymeStructure And Function RelasionshipMaize Sorghum Ricehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Malic enzyme is present in many plant cell compartments such as plastids, cytosol and mitochondria. Particularly relevant is the plastidial isoform that participates in the C4 cycle providing CO2 to RuBisCO in C4 species. This type of photosynthesis is more frequent among grasses where anatomical preconditioning would have facilitated the evolution of the C4 syndrome. In maize (C4 grass), the photosynthetic NADP dependent Malic enzyme (ZmC4-NADP-ME, L-malate:NADP oxidoreductase, E.C. 1.1.1.40) and the closest related non-photosynthetic isoform (ZmnonC4-NADPME, L-malate:NADP oxidoreductase, E.C. 1.1.1.40) are both plastidial but differ in expression pattern,kinetics and structure. Features like high catalytic efficiency, inhibition by high malate concentration at pH 7.0, redox modulation and tetramerization are characteristic of the photosynthetic NADP-ME. In this work, the proteins encoded by sorghum (C4 grass) and rice (C3 grass) NADP-ME genes,orthologues of the plastidial NADP-MEs from maize, were recombinantly expressed, purified and characterized. In a global comparison, we could identify a small group of residues which may explain the special features of C4 enzymes. Overall, the present work presents biochemical and molecular data that helps to elucidate the changes that took place in the evolution of C4 NADP-ME in grasses.Fil: Saigo, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; ArgentinaFil: Alvarez, Clarisa Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; ArgentinaFil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; ArgentinaFil: Drincovich, Maria Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; ArgentinaElsevier France-editions Scientifiques Medicales Elsevier2013-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/3418Saigo, Mariana; Alvarez, Clarisa Ester; Andreo, Carlos Santiago; Drincovich, Maria Fabiana; Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoforms; Elsevier France-editions Scientifiques Medicales Elsevier; Plant Physiology And Biochemistry; 63; 2-2013; 39-480981-9428enginfo:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/altIdentifier/doi/10.1016/j.plaphy.2012.11.009info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:47:21Zoai:ri.conicet.gov.ar:11336/3418instacron: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:34982025-09-29 10:47:21.755CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoforms
title Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoforms
spellingShingle Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoforms
Saigo, Mariana
C4 Photosynthesis
Nadp-Malic Enzyme
Structure And Function Relasionship
Maize Sorghum Rice
title_short Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoforms
title_full Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoforms
title_fullStr Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoforms
title_full_unstemmed Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoforms
title_sort Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoforms
dc.creator.none.fl_str_mv Saigo, Mariana
Alvarez, Clarisa Ester
Andreo, Carlos Santiago
Drincovich, Maria Fabiana
author Saigo, Mariana
author_facet Saigo, Mariana
Alvarez, Clarisa Ester
Andreo, Carlos Santiago
Drincovich, Maria Fabiana
author_role author
author2 Alvarez, Clarisa Ester
Andreo, Carlos Santiago
Drincovich, Maria Fabiana
author2_role author
author
author
dc.subject.none.fl_str_mv C4 Photosynthesis
Nadp-Malic Enzyme
Structure And Function Relasionship
Maize Sorghum Rice
topic C4 Photosynthesis
Nadp-Malic Enzyme
Structure And Function Relasionship
Maize Sorghum Rice
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Malic enzyme is present in many plant cell compartments such as plastids, cytosol and mitochondria. Particularly relevant is the plastidial isoform that participates in the C4 cycle providing CO2 to RuBisCO in C4 species. This type of photosynthesis is more frequent among grasses where anatomical preconditioning would have facilitated the evolution of the C4 syndrome. In maize (C4 grass), the photosynthetic NADP dependent Malic enzyme (ZmC4-NADP-ME, L-malate:NADP oxidoreductase, E.C. 1.1.1.40) and the closest related non-photosynthetic isoform (ZmnonC4-NADPME, L-malate:NADP oxidoreductase, E.C. 1.1.1.40) are both plastidial but differ in expression pattern,kinetics and structure. Features like high catalytic efficiency, inhibition by high malate concentration at pH 7.0, redox modulation and tetramerization are characteristic of the photosynthetic NADP-ME. In this work, the proteins encoded by sorghum (C4 grass) and rice (C3 grass) NADP-ME genes,orthologues of the plastidial NADP-MEs from maize, were recombinantly expressed, purified and characterized. In a global comparison, we could identify a small group of residues which may explain the special features of C4 enzymes. Overall, the present work presents biochemical and molecular data that helps to elucidate the changes that took place in the evolution of C4 NADP-ME in grasses.
Fil: Saigo, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
Fil: Alvarez, Clarisa Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
Fil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
Fil: Drincovich, Maria Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
description Malic enzyme is present in many plant cell compartments such as plastids, cytosol and mitochondria. Particularly relevant is the plastidial isoform that participates in the C4 cycle providing CO2 to RuBisCO in C4 species. This type of photosynthesis is more frequent among grasses where anatomical preconditioning would have facilitated the evolution of the C4 syndrome. In maize (C4 grass), the photosynthetic NADP dependent Malic enzyme (ZmC4-NADP-ME, L-malate:NADP oxidoreductase, E.C. 1.1.1.40) and the closest related non-photosynthetic isoform (ZmnonC4-NADPME, L-malate:NADP oxidoreductase, E.C. 1.1.1.40) are both plastidial but differ in expression pattern,kinetics and structure. Features like high catalytic efficiency, inhibition by high malate concentration at pH 7.0, redox modulation and tetramerization are characteristic of the photosynthetic NADP-ME. In this work, the proteins encoded by sorghum (C4 grass) and rice (C3 grass) NADP-ME genes,orthologues of the plastidial NADP-MEs from maize, were recombinantly expressed, purified and characterized. In a global comparison, we could identify a small group of residues which may explain the special features of C4 enzymes. Overall, the present work presents biochemical and molecular data that helps to elucidate the changes that took place in the evolution of C4 NADP-ME in grasses.
publishDate 2013
dc.date.none.fl_str_mv 2013-02
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/11336/3418
Saigo, Mariana; Alvarez, Clarisa Ester; Andreo, Carlos Santiago; Drincovich, Maria Fabiana; Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoforms; Elsevier France-editions Scientifiques Medicales Elsevier; Plant Physiology And Biochemistry; 63; 2-2013; 39-48
0981-9428
url http://hdl.handle.net/11336/3418
identifier_str_mv Saigo, Mariana; Alvarez, Clarisa Ester; Andreo, Carlos Santiago; Drincovich, Maria Fabiana; Plastidial NADP-Malic Enzymes from grasses: unravelling the way to the C4 specific isoforms; Elsevier France-editions Scientifiques Medicales Elsevier; Plant Physiology And Biochemistry; 63; 2-2013; 39-48
0981-9428
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.plaphy.2012.11.009
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier France-editions Scientifiques Medicales Elsevier
publisher.none.fl_str_mv Elsevier France-editions Scientifiques Medicales Elsevier
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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