Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity
- Autores
- Alvarez, Clarisa Ester; Detarsio, Enrique; Moreno, Silvia Margarita; Andreo, Carlos Santiago; Drincovich, Maria Fabiana
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Two highly similar plastidic NADP-malic enzymes (NADP-MEs) are found in the C 4 species maize (Zea mays); one exclusively expressed in the bundle sheath cells (BSCs) and involved in C 4 photosynthesis (ZmC 4-NADP-ME); and the other (ZmnonC 4-NADP-ME) with housekeeping roles. In the present work, these two NADP-MEs were analyzed regarding their redox-dependent activity modulation. The results clearly show that ZmC 4-NADP-ME is the only one modulated by redox status, and that its oxidation produces a conformational change limiting the catalytic process, although inducing higher affinity binding of the substrates. The reversal of ZmC 4-NADP-ME oxidation by chemical reductants suggests the presence of thiol groups able to form disulfide bonds. In order to identify the cysteine residues involved in the activity modulation, site-directed mutagenesis and MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) analysis of ZmC 4-NADP-ME were performed. The results obtained allowed the identification of Cys192, Cys246 (not conserved in ZmnonC 4-NADP-ME), Cys270 and Cys410 as directly or indirectly implicated in ZmC 4-NADP-ME redox modulation. These residues may be involved in forming disulfide bridge(s) or in the modulation of the oxidation of critical residues. Overall, the results indicate that, besides having acquired a high level of expression and localization in BSCs, ZmC 4-NADP-ME displays a particular redox modulation, which may be required to accomplish the C 4 photosynthetic metabolism. Therefore, the present work could provide new insights into the regulatory mechanisms potentially involved in the recruitment of genes for the C 4 pathway during evolution. © 2012 The Author.
Fil: Alvarez, Clarisa Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
Fil: Detarsio, Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
Fil: Moreno, Silvia Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmaceuticas. Departamento de Química Biologica; Argentina
Fil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
Fil: Drincovich, Maria Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina - Materia
-
C 4 PHOTOSYNTHESIS
MAIZE
NADP-MALIC ENZYME
REDOX MODULATION
STRUCTURE-FUNCTION RELATIONSHIP - 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:11336/61354
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Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activityAlvarez, Clarisa EsterDetarsio, EnriqueMoreno, Silvia MargaritaAndreo, Carlos SantiagoDrincovich, Maria FabianaC 4 PHOTOSYNTHESISMAIZENADP-MALIC ENZYMEREDOX MODULATIONSTRUCTURE-FUNCTION RELATIONSHIPhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Two highly similar plastidic NADP-malic enzymes (NADP-MEs) are found in the C 4 species maize (Zea mays); one exclusively expressed in the bundle sheath cells (BSCs) and involved in C 4 photosynthesis (ZmC 4-NADP-ME); and the other (ZmnonC 4-NADP-ME) with housekeeping roles. In the present work, these two NADP-MEs were analyzed regarding their redox-dependent activity modulation. The results clearly show that ZmC 4-NADP-ME is the only one modulated by redox status, and that its oxidation produces a conformational change limiting the catalytic process, although inducing higher affinity binding of the substrates. The reversal of ZmC 4-NADP-ME oxidation by chemical reductants suggests the presence of thiol groups able to form disulfide bonds. In order to identify the cysteine residues involved in the activity modulation, site-directed mutagenesis and MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) analysis of ZmC 4-NADP-ME were performed. The results obtained allowed the identification of Cys192, Cys246 (not conserved in ZmnonC 4-NADP-ME), Cys270 and Cys410 as directly or indirectly implicated in ZmC 4-NADP-ME redox modulation. These residues may be involved in forming disulfide bridge(s) or in the modulation of the oxidation of critical residues. Overall, the results indicate that, besides having acquired a high level of expression and localization in BSCs, ZmC 4-NADP-ME displays a particular redox modulation, which may be required to accomplish the C 4 photosynthetic metabolism. Therefore, the present work could provide new insights into the regulatory mechanisms potentially involved in the recruitment of genes for the C 4 pathway during evolution. © 2012 The Author.Fil: Alvarez, Clarisa Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Detarsio, Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Moreno, Silvia Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmaceuticas. Departamento de Química Biologica; ArgentinaFil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Drincovich, Maria Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaOxford University Press2012-06info: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/11336/61354Alvarez, Clarisa Ester; Detarsio, Enrique; Moreno, Silvia Margarita; Andreo, Carlos Santiago; Drincovich, Maria Fabiana; Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity; Oxford University Press; Plant And Cell Physiology; 53; 6; 6-2012; 1144-11530032-0781CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1093/pcp/pcs059info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/pcp/article/53/6/1144/1809330info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:50:40Zoai:ri.conicet.gov.ar:11336/61354instacron: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 09:50:41.063CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity |
title |
Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity |
spellingShingle |
Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity Alvarez, Clarisa Ester C 4 PHOTOSYNTHESIS MAIZE NADP-MALIC ENZYME REDOX MODULATION STRUCTURE-FUNCTION RELATIONSHIP |
title_short |
Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity |
title_full |
Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity |
title_fullStr |
Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity |
title_full_unstemmed |
Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity |
title_sort |
Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity |
dc.creator.none.fl_str_mv |
Alvarez, Clarisa Ester Detarsio, Enrique Moreno, Silvia Margarita Andreo, Carlos Santiago Drincovich, Maria Fabiana |
author |
Alvarez, Clarisa Ester |
author_facet |
Alvarez, Clarisa Ester Detarsio, Enrique Moreno, Silvia Margarita Andreo, Carlos Santiago Drincovich, Maria Fabiana |
author_role |
author |
author2 |
Detarsio, Enrique Moreno, Silvia Margarita Andreo, Carlos Santiago Drincovich, Maria Fabiana |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
C 4 PHOTOSYNTHESIS MAIZE NADP-MALIC ENZYME REDOX MODULATION STRUCTURE-FUNCTION RELATIONSHIP |
topic |
C 4 PHOTOSYNTHESIS MAIZE NADP-MALIC ENZYME REDOX MODULATION STRUCTURE-FUNCTION RELATIONSHIP |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Two highly similar plastidic NADP-malic enzymes (NADP-MEs) are found in the C 4 species maize (Zea mays); one exclusively expressed in the bundle sheath cells (BSCs) and involved in C 4 photosynthesis (ZmC 4-NADP-ME); and the other (ZmnonC 4-NADP-ME) with housekeeping roles. In the present work, these two NADP-MEs were analyzed regarding their redox-dependent activity modulation. The results clearly show that ZmC 4-NADP-ME is the only one modulated by redox status, and that its oxidation produces a conformational change limiting the catalytic process, although inducing higher affinity binding of the substrates. The reversal of ZmC 4-NADP-ME oxidation by chemical reductants suggests the presence of thiol groups able to form disulfide bonds. In order to identify the cysteine residues involved in the activity modulation, site-directed mutagenesis and MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) analysis of ZmC 4-NADP-ME were performed. The results obtained allowed the identification of Cys192, Cys246 (not conserved in ZmnonC 4-NADP-ME), Cys270 and Cys410 as directly or indirectly implicated in ZmC 4-NADP-ME redox modulation. These residues may be involved in forming disulfide bridge(s) or in the modulation of the oxidation of critical residues. Overall, the results indicate that, besides having acquired a high level of expression and localization in BSCs, ZmC 4-NADP-ME displays a particular redox modulation, which may be required to accomplish the C 4 photosynthetic metabolism. Therefore, the present work could provide new insights into the regulatory mechanisms potentially involved in the recruitment of genes for the C 4 pathway during evolution. © 2012 The Author. Fil: Alvarez, Clarisa Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Detarsio, Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Moreno, Silvia Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmaceuticas. Departamento de Química Biologica; Argentina Fil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Drincovich, Maria Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina |
description |
Two highly similar plastidic NADP-malic enzymes (NADP-MEs) are found in the C 4 species maize (Zea mays); one exclusively expressed in the bundle sheath cells (BSCs) and involved in C 4 photosynthesis (ZmC 4-NADP-ME); and the other (ZmnonC 4-NADP-ME) with housekeeping roles. In the present work, these two NADP-MEs were analyzed regarding their redox-dependent activity modulation. The results clearly show that ZmC 4-NADP-ME is the only one modulated by redox status, and that its oxidation produces a conformational change limiting the catalytic process, although inducing higher affinity binding of the substrates. The reversal of ZmC 4-NADP-ME oxidation by chemical reductants suggests the presence of thiol groups able to form disulfide bonds. In order to identify the cysteine residues involved in the activity modulation, site-directed mutagenesis and MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) analysis of ZmC 4-NADP-ME were performed. The results obtained allowed the identification of Cys192, Cys246 (not conserved in ZmnonC 4-NADP-ME), Cys270 and Cys410 as directly or indirectly implicated in ZmC 4-NADP-ME redox modulation. These residues may be involved in forming disulfide bridge(s) or in the modulation of the oxidation of critical residues. Overall, the results indicate that, besides having acquired a high level of expression and localization in BSCs, ZmC 4-NADP-ME displays a particular redox modulation, which may be required to accomplish the C 4 photosynthetic metabolism. Therefore, the present work could provide new insights into the regulatory mechanisms potentially involved in the recruitment of genes for the C 4 pathway during evolution. © 2012 The Author. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-06 |
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/11336/61354 Alvarez, Clarisa Ester; Detarsio, Enrique; Moreno, Silvia Margarita; Andreo, Carlos Santiago; Drincovich, Maria Fabiana; Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity; Oxford University Press; Plant And Cell Physiology; 53; 6; 6-2012; 1144-1153 0032-0781 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/61354 |
identifier_str_mv |
Alvarez, Clarisa Ester; Detarsio, Enrique; Moreno, Silvia Margarita; Andreo, Carlos Santiago; Drincovich, Maria Fabiana; Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity; Oxford University Press; Plant And Cell Physiology; 53; 6; 6-2012; 1144-1153 0032-0781 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1093/pcp/pcs059 info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/pcp/article/53/6/1144/1809330 |
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 application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Oxford University Press |
publisher.none.fl_str_mv |
Oxford University Press |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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13.070432 |