Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues

Autores
Meringer, Maria Veronica; Villasuso, Ana Laura; Pasquaré, Susana Juana; Giusto, Norma Maria; Machado, Estela Edelmira; Racagni, Graciela Esther
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We analyzed lipid kinase and lipid phosphatase activities and determined endogenous phytohormone levels by liquid chromatography–tandem mass spectrometry in root and coleoptile tissues following germination of barley (Hordeum vulgare) seeds. The enzymes showing highest activity in aleurone cells were diacylglycerol kinase (DAG-k, EC 2.7.1.107) and phosphatidate kinase (PA-k). The ratio of gibberellins (GAs) to abscisic acid (ABA) was 2-fold higher in aleurone than in coleoptile or root tissues. In coleoptiles, phosphatidylinositol 4-kinase (PI4-k, EC 2.7.1.67) showed the highest enzyme activity, and jasmonic acid (JA) level was higher than in aleurone. In roots, activities of PI4-k, DAG-k, and PA-k were similar, and salicylic acid (SA) showed the highest concentration. In the assays to evaluate the hydrolysis of DGPP (diacylglycerol pyrophosphate) and PA (phosphatidic acid) we observed that PA hydrolysis by LPPs (lipid phosphate phosphatases) was not modified; however, the diacylglycerol pyrophosphate phosphatase (DGPPase) was strikingly higher in coleoptile and root tissues than to aleurone. Relevance of these findings in terms of signaling responses and seedling growth is discussed.
Fil: Meringer, Maria Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Cuarto; Argentina
Fil: Villasuso, Ana Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Cuarto; Argentina
Fil: Pasquaré, Susana Juana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Giusto, Norma Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Machado, Estela Edelmira. Universidad Nacional de Río Cuarto; Argentina
Fil: Racagni, Graciela Esther. Universidad Nacional de Río Cuarto; Argentina
Materia
Barley
Lipid Kinases
Lipid Phosphate Phoshatases
Phospholipids
Phytohormones
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:11336/44876

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oai_identifier_str oai:ri.conicet.gov.ar:11336/44876
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissuesMeringer, Maria VeronicaVillasuso, Ana LauraPasquaré, Susana JuanaGiusto, Norma MariaMachado, Estela EdelmiraRacagni, Graciela EstherBarleyLipid KinasesLipid Phosphate PhoshatasesPhospholipidsPhytohormoneshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We analyzed lipid kinase and lipid phosphatase activities and determined endogenous phytohormone levels by liquid chromatography–tandem mass spectrometry in root and coleoptile tissues following germination of barley (Hordeum vulgare) seeds. The enzymes showing highest activity in aleurone cells were diacylglycerol kinase (DAG-k, EC 2.7.1.107) and phosphatidate kinase (PA-k). The ratio of gibberellins (GAs) to abscisic acid (ABA) was 2-fold higher in aleurone than in coleoptile or root tissues. In coleoptiles, phosphatidylinositol 4-kinase (PI4-k, EC 2.7.1.67) showed the highest enzyme activity, and jasmonic acid (JA) level was higher than in aleurone. In roots, activities of PI4-k, DAG-k, and PA-k were similar, and salicylic acid (SA) showed the highest concentration. In the assays to evaluate the hydrolysis of DGPP (diacylglycerol pyrophosphate) and PA (phosphatidic acid) we observed that PA hydrolysis by LPPs (lipid phosphate phosphatases) was not modified; however, the diacylglycerol pyrophosphate phosphatase (DGPPase) was strikingly higher in coleoptile and root tissues than to aleurone. Relevance of these findings in terms of signaling responses and seedling growth is discussed.Fil: Meringer, Maria Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Cuarto; ArgentinaFil: Villasuso, Ana Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Cuarto; ArgentinaFil: Pasquaré, Susana Juana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Giusto, Norma Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Machado, Estela Edelmira. Universidad Nacional de Río Cuarto; ArgentinaFil: Racagni, Graciela Esther. Universidad Nacional de Río Cuarto; ArgentinaElsevier France-editions Scientifiques Medicales Elsevier2012-06-23info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/44876Meringer, Maria Veronica; Villasuso, Ana Laura; Pasquaré, Susana Juana; Giusto, Norma Maria; Machado, Estela Edelmira; et al.; Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues; Elsevier France-editions Scientifiques Medicales Elsevier; Plant Physiology and Biochemistry; 58; 23-6-2012; 83-880981-9428CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0981942812001556info:eu-repo/semantics/altIdentifier/doi/10.1016/j.plaphy.2012.06.013info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:42:20Zoai:ri.conicet.gov.ar:11336/44876instacron: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 09:42:20.383CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues
title Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues
spellingShingle Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues
Meringer, Maria Veronica
Barley
Lipid Kinases
Lipid Phosphate Phoshatases
Phospholipids
Phytohormones
title_short Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues
title_full Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues
title_fullStr Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues
title_full_unstemmed Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues
title_sort Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues
dc.creator.none.fl_str_mv Meringer, Maria Veronica
Villasuso, Ana Laura
Pasquaré, Susana Juana
Giusto, Norma Maria
Machado, Estela Edelmira
Racagni, Graciela Esther
author Meringer, Maria Veronica
author_facet Meringer, Maria Veronica
Villasuso, Ana Laura
Pasquaré, Susana Juana
Giusto, Norma Maria
Machado, Estela Edelmira
Racagni, Graciela Esther
author_role author
author2 Villasuso, Ana Laura
Pasquaré, Susana Juana
Giusto, Norma Maria
Machado, Estela Edelmira
Racagni, Graciela Esther
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Barley
Lipid Kinases
Lipid Phosphate Phoshatases
Phospholipids
Phytohormones
topic Barley
Lipid Kinases
Lipid Phosphate Phoshatases
Phospholipids
Phytohormones
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv We analyzed lipid kinase and lipid phosphatase activities and determined endogenous phytohormone levels by liquid chromatography–tandem mass spectrometry in root and coleoptile tissues following germination of barley (Hordeum vulgare) seeds. The enzymes showing highest activity in aleurone cells were diacylglycerol kinase (DAG-k, EC 2.7.1.107) and phosphatidate kinase (PA-k). The ratio of gibberellins (GAs) to abscisic acid (ABA) was 2-fold higher in aleurone than in coleoptile or root tissues. In coleoptiles, phosphatidylinositol 4-kinase (PI4-k, EC 2.7.1.67) showed the highest enzyme activity, and jasmonic acid (JA) level was higher than in aleurone. In roots, activities of PI4-k, DAG-k, and PA-k were similar, and salicylic acid (SA) showed the highest concentration. In the assays to evaluate the hydrolysis of DGPP (diacylglycerol pyrophosphate) and PA (phosphatidic acid) we observed that PA hydrolysis by LPPs (lipid phosphate phosphatases) was not modified; however, the diacylglycerol pyrophosphate phosphatase (DGPPase) was strikingly higher in coleoptile and root tissues than to aleurone. Relevance of these findings in terms of signaling responses and seedling growth is discussed.
Fil: Meringer, Maria Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Cuarto; Argentina
Fil: Villasuso, Ana Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Cuarto; Argentina
Fil: Pasquaré, Susana Juana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Giusto, Norma Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Machado, Estela Edelmira. Universidad Nacional de Río Cuarto; Argentina
Fil: Racagni, Graciela Esther. Universidad Nacional de Río Cuarto; Argentina
description We analyzed lipid kinase and lipid phosphatase activities and determined endogenous phytohormone levels by liquid chromatography–tandem mass spectrometry in root and coleoptile tissues following germination of barley (Hordeum vulgare) seeds. The enzymes showing highest activity in aleurone cells were diacylglycerol kinase (DAG-k, EC 2.7.1.107) and phosphatidate kinase (PA-k). The ratio of gibberellins (GAs) to abscisic acid (ABA) was 2-fold higher in aleurone than in coleoptile or root tissues. In coleoptiles, phosphatidylinositol 4-kinase (PI4-k, EC 2.7.1.67) showed the highest enzyme activity, and jasmonic acid (JA) level was higher than in aleurone. In roots, activities of PI4-k, DAG-k, and PA-k were similar, and salicylic acid (SA) showed the highest concentration. In the assays to evaluate the hydrolysis of DGPP (diacylglycerol pyrophosphate) and PA (phosphatidic acid) we observed that PA hydrolysis by LPPs (lipid phosphate phosphatases) was not modified; however, the diacylglycerol pyrophosphate phosphatase (DGPPase) was strikingly higher in coleoptile and root tissues than to aleurone. Relevance of these findings in terms of signaling responses and seedling growth is discussed.
publishDate 2012
dc.date.none.fl_str_mv 2012-06-23
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/11336/44876
Meringer, Maria Veronica; Villasuso, Ana Laura; Pasquaré, Susana Juana; Giusto, Norma Maria; Machado, Estela Edelmira; et al.; Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues; Elsevier France-editions Scientifiques Medicales Elsevier; Plant Physiology and Biochemistry; 58; 23-6-2012; 83-88
0981-9428
CONICET Digital
CONICET
url http://hdl.handle.net/11336/44876
identifier_str_mv Meringer, Maria Veronica; Villasuso, Ana Laura; Pasquaré, Susana Juana; Giusto, Norma Maria; Machado, Estela Edelmira; et al.; Comparative phytohormone pro les, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues; Elsevier France-editions Scientifiques Medicales Elsevier; Plant Physiology and Biochemistry; 58; 23-6-2012; 83-88
0981-9428
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0981942812001556
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.plaphy.2012.06.013
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
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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