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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/3418
Ver los metadatos del registro completo
id |
CONICETDig_e3a2e099a656245892df2e3666f02f42 |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/3418 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
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 |
_version_ |
1844614517245345792 |
score |
13.070432 |