Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of Arabidopsis

Autores
Monteoliva, Mariela Inés; Rizzi, Yanina; Cecchini, Nicolas Miguel; Hajirezaei, Mohammad Reza; Alvarez, Maria Elena
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Background:Proline (Pro) dehydrogenase (ProDH) potentiates the oxidative burst and cell death of the plantHypersensitive Response (HR) by mechanisms not yet elucidated. ProDH converts Pro intoΔ1pyrroline-5-carboxylate(P5C) and can act together with P5C dehydrogenase (P5CDH) to produce Glu, or with P5C reductase (P5CR) toregenerate Pro and thus stimulate the Pro/P5C cycle. To better understand the effects of ProDH in HR, we studiedtheenzymeatthreestagesofthedefenseresponsediffering in their ROS and cell death levels. In addition, wetested if ProDH requires P5CDH to potentiate HR.Results:Control and infected leaves of wild type andp5cdhplants were used to monitor ProDH activity,in vivoPro catabolism, amino acid content, and gene expression. Wild type plants activated ProDH at all HR stages. Theydid not consume Pro during maximal ROS accumulation, and maintained almost basal P5C levels at all conditions.p5cdhmutants activated ProDH as wild type plants. They achieved maximum oxidative burst and cell death levelsproducing normal HR lesions, but evidenced premature defense activation.Conclusion:ProDH activation has different effects on HR. Before the oxidative burst it leads to Pro consumptioninvolving the action of P5CDH. During the oxidative burst, ProDH becomes functionally uncoupled to P5CDH andapparently works with P5CR. The absence of P5CDH does not reduce ROS, cell death, or pathogen resistance, indicatingthis enzyme is not accompanying ProDH in the potentiation of these defense responses. In contrast,p5cdhinfectedplants displayed increased ROS burst and earlier initiation of HR cell death. In turn, our results suggest that ProDH maysustain HR by participating in the Pro/P5C cycle, whose action on HR must be formally evaluated in a future.
Fil: Monteoliva, Mariela Inés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Rizzi, Yanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Cecchini, Nicolas Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Hajirezaei, Mohammad Reza. Leibniz Institute of Plant Genetics and Crop Plant Research. Gatersleben; Alemania
Fil: Alvarez, Maria Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Materia
Proline metabolism
Proline dehydrogenase/oxidase
P5C
Stress responses
Arabidopsis
Pseudomonassyringae
Hypersensitive Response
Cell death
Reactive oxygen species (ROS)
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:11336/32115
Acceder
id CONICETDig_18870fb959067a38bed6af8772d1f7d7
oai_identifier_str oai:ri.conicet.gov.ar:11336/32115
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of ArabidopsisMonteoliva, Mariela InésRizzi, YaninaCecchini, Nicolas MiguelHajirezaei, Mohammad RezaAlvarez, Maria ElenaProline metabolismProline dehydrogenase/oxidaseP5CStress responsesArabidopsisPseudomonassyringaeHypersensitive ResponseCell deathReactive oxygen species (ROS)https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Background:Proline (Pro) dehydrogenase (ProDH) potentiates the oxidative burst and cell death of the plantHypersensitive Response (HR) by mechanisms not yet elucidated. ProDH converts Pro intoΔ1pyrroline-5-carboxylate(P5C) and can act together with P5C dehydrogenase (P5CDH) to produce Glu, or with P5C reductase (P5CR) toregenerate Pro and thus stimulate the Pro/P5C cycle. To better understand the effects of ProDH in HR, we studiedtheenzymeatthreestagesofthedefenseresponsediffering in their ROS and cell death levels. In addition, wetested if ProDH requires P5CDH to potentiate HR.Results:Control and infected leaves of wild type andp5cdhplants were used to monitor ProDH activity,in vivoPro catabolism, amino acid content, and gene expression. Wild type plants activated ProDH at all HR stages. Theydid not consume Pro during maximal ROS accumulation, and maintained almost basal P5C levels at all conditions.p5cdhmutants activated ProDH as wild type plants. They achieved maximum oxidative burst and cell death levelsproducing normal HR lesions, but evidenced premature defense activation.Conclusion:ProDH activation has different effects on HR. Before the oxidative burst it leads to Pro consumptioninvolving the action of P5CDH. During the oxidative burst, ProDH becomes functionally uncoupled to P5CDH andapparently works with P5CR. The absence of P5CDH does not reduce ROS, cell death, or pathogen resistance, indicatingthis enzyme is not accompanying ProDH in the potentiation of these defense responses. In contrast,p5cdhinfectedplants displayed increased ROS burst and earlier initiation of HR cell death. In turn, our results suggest that ProDH maysustain HR by participating in the Pro/P5C cycle, whose action on HR must be formally evaluated in a future.Fil: Monteoliva, Mariela Inés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Rizzi, Yanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Cecchini, Nicolas Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Hajirezaei, Mohammad Reza. Leibniz Institute of Plant Genetics and Crop Plant Research. Gatersleben; AlemaniaFil: Alvarez, Maria Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaBioMed Central2014-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/32115Alvarez, Maria Elena; Hajirezaei, Mohammad Reza; Cecchini, Nicolas Miguel; Rizzi, Yanina; Monteoliva, Mariela Inés; Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of Arabidopsis; BioMed Central; BMC Plant Biology; 14; 1-2014; 21-321471-2229CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1186/1471-2229-14-21info:eu-repo/semantics/altIdentifier/url/https://bmcplantbiol.biomedcentral.com/articles/10.1186/1471-2229-14-21info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:26:33Zoai:ri.conicet.gov.ar:11336/32115instacron: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 10:26:34.202CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of Arabidopsis
title Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of Arabidopsis
spellingShingle Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of Arabidopsis
Monteoliva, Mariela Inés
Proline metabolism
Proline dehydrogenase/oxidase
P5C
Stress responses
Arabidopsis
Pseudomonassyringae
Hypersensitive Response
Cell death
Reactive oxygen species (ROS)
title_short Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of Arabidopsis
title_full Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of Arabidopsis
title_fullStr Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of Arabidopsis
title_full_unstemmed Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of Arabidopsis
title_sort Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of Arabidopsis
dc.creator.none.fl_str_mv Monteoliva, Mariela Inés
Rizzi, Yanina
Cecchini, Nicolas Miguel
Hajirezaei, Mohammad Reza
Alvarez, Maria Elena
author Monteoliva, Mariela Inés
author_facet Monteoliva, Mariela Inés
Rizzi, Yanina
Cecchini, Nicolas Miguel
Hajirezaei, Mohammad Reza
Alvarez, Maria Elena
author_role author
author2 Rizzi, Yanina
Cecchini, Nicolas Miguel
Hajirezaei, Mohammad Reza
Alvarez, Maria Elena
author2_role author
author
author
author
dc.subject.none.fl_str_mv Proline metabolism
Proline dehydrogenase/oxidase
P5C
Stress responses
Arabidopsis
Pseudomonassyringae
Hypersensitive Response
Cell death
Reactive oxygen species (ROS)
topic Proline metabolism
Proline dehydrogenase/oxidase
P5C
Stress responses
Arabidopsis
Pseudomonassyringae
Hypersensitive Response
Cell death
Reactive oxygen species (ROS)
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Background:Proline (Pro) dehydrogenase (ProDH) potentiates the oxidative burst and cell death of the plantHypersensitive Response (HR) by mechanisms not yet elucidated. ProDH converts Pro intoΔ1pyrroline-5-carboxylate(P5C) and can act together with P5C dehydrogenase (P5CDH) to produce Glu, or with P5C reductase (P5CR) toregenerate Pro and thus stimulate the Pro/P5C cycle. To better understand the effects of ProDH in HR, we studiedtheenzymeatthreestagesofthedefenseresponsediffering in their ROS and cell death levels. In addition, wetested if ProDH requires P5CDH to potentiate HR.Results:Control and infected leaves of wild type andp5cdhplants were used to monitor ProDH activity,in vivoPro catabolism, amino acid content, and gene expression. Wild type plants activated ProDH at all HR stages. Theydid not consume Pro during maximal ROS accumulation, and maintained almost basal P5C levels at all conditions.p5cdhmutants activated ProDH as wild type plants. They achieved maximum oxidative burst and cell death levelsproducing normal HR lesions, but evidenced premature defense activation.Conclusion:ProDH activation has different effects on HR. Before the oxidative burst it leads to Pro consumptioninvolving the action of P5CDH. During the oxidative burst, ProDH becomes functionally uncoupled to P5CDH andapparently works with P5CR. The absence of P5CDH does not reduce ROS, cell death, or pathogen resistance, indicatingthis enzyme is not accompanying ProDH in the potentiation of these defense responses. In contrast,p5cdhinfectedplants displayed increased ROS burst and earlier initiation of HR cell death. In turn, our results suggest that ProDH maysustain HR by participating in the Pro/P5C cycle, whose action on HR must be formally evaluated in a future.
Fil: Monteoliva, Mariela Inés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Rizzi, Yanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Cecchini, Nicolas Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Hajirezaei, Mohammad Reza. Leibniz Institute of Plant Genetics and Crop Plant Research. Gatersleben; Alemania
Fil: Alvarez, Maria Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
description Background:Proline (Pro) dehydrogenase (ProDH) potentiates the oxidative burst and cell death of the plantHypersensitive Response (HR) by mechanisms not yet elucidated. ProDH converts Pro intoΔ1pyrroline-5-carboxylate(P5C) and can act together with P5C dehydrogenase (P5CDH) to produce Glu, or with P5C reductase (P5CR) toregenerate Pro and thus stimulate the Pro/P5C cycle. To better understand the effects of ProDH in HR, we studiedtheenzymeatthreestagesofthedefenseresponsediffering in their ROS and cell death levels. In addition, wetested if ProDH requires P5CDH to potentiate HR.Results:Control and infected leaves of wild type andp5cdhplants were used to monitor ProDH activity,in vivoPro catabolism, amino acid content, and gene expression. Wild type plants activated ProDH at all HR stages. Theydid not consume Pro during maximal ROS accumulation, and maintained almost basal P5C levels at all conditions.p5cdhmutants activated ProDH as wild type plants. They achieved maximum oxidative burst and cell death levelsproducing normal HR lesions, but evidenced premature defense activation.Conclusion:ProDH activation has different effects on HR. Before the oxidative burst it leads to Pro consumptioninvolving the action of P5CDH. During the oxidative burst, ProDH becomes functionally uncoupled to P5CDH andapparently works with P5CR. The absence of P5CDH does not reduce ROS, cell death, or pathogen resistance, indicatingthis enzyme is not accompanying ProDH in the potentiation of these defense responses. In contrast,p5cdhinfectedplants displayed increased ROS burst and earlier initiation of HR cell death. In turn, our results suggest that ProDH maysustain HR by participating in the Pro/P5C cycle, whose action on HR must be formally evaluated in a future.
publishDate 2014
dc.date.none.fl_str_mv 2014-01
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/11336/32115
Alvarez, Maria Elena; Hajirezaei, Mohammad Reza; Cecchini, Nicolas Miguel; Rizzi, Yanina; Monteoliva, Mariela Inés; Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of Arabidopsis; BioMed Central; BMC Plant Biology; 14; 1-2014; 21-32
1471-2229
CONICET Digital
CONICET
url http://hdl.handle.net/11336/32115
identifier_str_mv Alvarez, Maria Elena; Hajirezaei, Mohammad Reza; Cecchini, Nicolas Miguel; Rizzi, Yanina; Monteoliva, Mariela Inés; Context of action of Proline Dehydrogenase (ProDH) in the Hypersensitive Response of Arabidopsis; BioMed Central; BMC Plant Biology; 14; 1-2014; 21-32
1471-2229
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1186/1471-2229-14-21
info:eu-repo/semantics/altIdentifier/url/https://bmcplantbiol.biomedcentral.com/articles/10.1186/1471-2229-14-21
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
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dc.publisher.none.fl_str_mv BioMed Central
publisher.none.fl_str_mv BioMed Central
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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