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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/44876
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oai:ri.conicet.gov.ar:11336/44876 |
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3498 |
network_name_str |
CONICET Digital (CONICET) |
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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 |
_version_ |
1844613333968224256 |
score |
13.070432 |