Calcium-dependent Protein Kinases are Involved in Potato Signal Transduction.

Autores
Blanco, F.A.; Zanetti, M.E.; Daleo, Gustavo Raúl
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión enviada
Descripción
Plant response to pathogens involves an intricate network of signal transduction pathways. Here, potato cell cultures were used to study signal transduction in response to elicitors fromPhytophthora infestans. Pretreatment of cells with Ser/Thr protein kinase inhibitors, EGTA, calmodulin antagonists or a channel blocker abolished the induction of two enzymes involved in defence responses, phenylalanine ammonia-lyase (PAL) and peroxidase. Phosphatase inhibitors caused an increase of these activities in the absence of elicitors. Hyphal cell wall components (HWC) from an incompatible race (HWC 0) produced a rapid and transient increment of histone phosphorylation, whereas induction by HWC from a compatible race (HWC C) was less pronounced and more sustained. As activities were calcium-dependent, a fraction enriched in calcium-dependent protein kinases (CDPKs) was obtained by DEAE chromatography. Fractions from HWC 0- and HWC C-treated cells presented higher kinase activity than that from untreated cells. Moreover, total activity was higher in the incompatible than in the compatible interaction. Activity was calcium-dependent, partially inhibited by calmodulin antagonists and able to phosphorylate syntide-2, a specific substrate of CDPKs. An in-gel kinase assay showed the presence of a band of approximately 50kDa whose activity was higher in HWC 0- than in HWC C-treated cells and was not detected in control extracts. This report presents evidences of the differential activation of CDPKs in response to elicitors from different races ofP. infestans, revealing that these protein kinases participate in the defence response to oomycete.
Materia
Bioquímica y Biología Molecular
Calmodulin
Cell culture
Peroxidase
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-nd/4.0/
Repositorio
CIC Digital (CICBA)
Institución
Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
OAI Identificador
oai:digital.cic.gba.gob.ar:11746/5606

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oai_identifier_str oai:digital.cic.gba.gob.ar:11746/5606
network_acronym_str CICBA
repository_id_str 9441
network_name_str CIC Digital (CICBA)
spelling Calcium-dependent Protein Kinases are Involved in Potato Signal Transduction.Blanco, F.A.Zanetti, M.E.Daleo, Gustavo RaúlBioquímica y Biología MolecularCalmodulinCell culturePeroxidasePlant response to pathogens involves an intricate network of signal transduction pathways. Here, potato cell cultures were used to study signal transduction in response to elicitors from<em>Phytophthora infestans</em>. Pretreatment of cells with Ser/Thr protein kinase inhibitors, EGTA, calmodulin antagonists or a channel blocker abolished the induction of two enzymes involved in defence responses, phenylalanine ammonia-lyase (PAL) and peroxidase. Phosphatase inhibitors caused an increase of these activities in the absence of elicitors. Hyphal cell wall components (HWC) from an incompatible race (HWC 0) produced a rapid and transient increment of histone phosphorylation, whereas induction by HWC from a compatible race (HWC C) was less pronounced and more sustained. As activities were calcium-dependent, a fraction enriched in calcium-dependent protein kinases (CDPKs) was obtained by DEAE chromatography. Fractions from HWC 0- and HWC C-treated cells presented higher kinase activity than that from untreated cells. Moreover, total activity was higher in the incompatible than in the compatible interaction. Activity was calcium-dependent, partially inhibited by calmodulin antagonists and able to phosphorylate syntide-2, a specific substrate of CDPKs. An in-gel kinase assay showed the presence of a band of approximately 50kDa whose activity was higher in HWC 0- than in HWC C-treated cells and was not detected in control extracts. This report presents evidences of the differential activation of CDPKs in response to elicitors from different races of<em>P. infestans</em>, revealing that these protein kinases participate in the defence response to oomycete.2008-01-30info:eu-repo/semantics/articleinfo:eu-repo/semantics/submittedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://digital.cic.gba.gob.ar/handle/11746/5606enginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/4.0/reponame:CIC Digital (CICBA)instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Airesinstacron:CICBA2025-10-30T11:18:28Zoai:digital.cic.gba.gob.ar:11746/5606Institucionalhttp://digital.cic.gba.gob.arOrganismo científico-tecnológicoNo correspondehttp://digital.cic.gba.gob.ar/oai/snrdmarisa.degiusti@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:94412025-10-30 11:18:28.974CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Airesfalse
dc.title.none.fl_str_mv Calcium-dependent Protein Kinases are Involved in Potato Signal Transduction.
title Calcium-dependent Protein Kinases are Involved in Potato Signal Transduction.
spellingShingle Calcium-dependent Protein Kinases are Involved in Potato Signal Transduction.
Blanco, F.A.
Bioquímica y Biología Molecular
Calmodulin
Cell culture
Peroxidase
title_short Calcium-dependent Protein Kinases are Involved in Potato Signal Transduction.
title_full Calcium-dependent Protein Kinases are Involved in Potato Signal Transduction.
title_fullStr Calcium-dependent Protein Kinases are Involved in Potato Signal Transduction.
title_full_unstemmed Calcium-dependent Protein Kinases are Involved in Potato Signal Transduction.
title_sort Calcium-dependent Protein Kinases are Involved in Potato Signal Transduction.
dc.creator.none.fl_str_mv Blanco, F.A.
Zanetti, M.E.
Daleo, Gustavo Raúl
author Blanco, F.A.
author_facet Blanco, F.A.
Zanetti, M.E.
Daleo, Gustavo Raúl
author_role author
author2 Zanetti, M.E.
Daleo, Gustavo Raúl
author2_role author
author
dc.subject.none.fl_str_mv Bioquímica y Biología Molecular
Calmodulin
Cell culture
Peroxidase
topic Bioquímica y Biología Molecular
Calmodulin
Cell culture
Peroxidase
dc.description.none.fl_txt_mv Plant response to pathogens involves an intricate network of signal transduction pathways. Here, potato cell cultures were used to study signal transduction in response to elicitors from<em>Phytophthora infestans</em>. Pretreatment of cells with Ser/Thr protein kinase inhibitors, EGTA, calmodulin antagonists or a channel blocker abolished the induction of two enzymes involved in defence responses, phenylalanine ammonia-lyase (PAL) and peroxidase. Phosphatase inhibitors caused an increase of these activities in the absence of elicitors. Hyphal cell wall components (HWC) from an incompatible race (HWC 0) produced a rapid and transient increment of histone phosphorylation, whereas induction by HWC from a compatible race (HWC C) was less pronounced and more sustained. As activities were calcium-dependent, a fraction enriched in calcium-dependent protein kinases (CDPKs) was obtained by DEAE chromatography. Fractions from HWC 0- and HWC C-treated cells presented higher kinase activity than that from untreated cells. Moreover, total activity was higher in the incompatible than in the compatible interaction. Activity was calcium-dependent, partially inhibited by calmodulin antagonists and able to phosphorylate syntide-2, a specific substrate of CDPKs. An in-gel kinase assay showed the presence of a band of approximately 50kDa whose activity was higher in HWC 0- than in HWC C-treated cells and was not detected in control extracts. This report presents evidences of the differential activation of CDPKs in response to elicitors from different races of<em>P. infestans</em>, revealing that these protein kinases participate in the defence response to oomycete.
description Plant response to pathogens involves an intricate network of signal transduction pathways. Here, potato cell cultures were used to study signal transduction in response to elicitors from<em>Phytophthora infestans</em>. Pretreatment of cells with Ser/Thr protein kinase inhibitors, EGTA, calmodulin antagonists or a channel blocker abolished the induction of two enzymes involved in defence responses, phenylalanine ammonia-lyase (PAL) and peroxidase. Phosphatase inhibitors caused an increase of these activities in the absence of elicitors. Hyphal cell wall components (HWC) from an incompatible race (HWC 0) produced a rapid and transient increment of histone phosphorylation, whereas induction by HWC from a compatible race (HWC C) was less pronounced and more sustained. As activities were calcium-dependent, a fraction enriched in calcium-dependent protein kinases (CDPKs) was obtained by DEAE chromatography. Fractions from HWC 0- and HWC C-treated cells presented higher kinase activity than that from untreated cells. Moreover, total activity was higher in the incompatible than in the compatible interaction. Activity was calcium-dependent, partially inhibited by calmodulin antagonists and able to phosphorylate syntide-2, a specific substrate of CDPKs. An in-gel kinase assay showed the presence of a band of approximately 50kDa whose activity was higher in HWC 0- than in HWC C-treated cells and was not detected in control extracts. This report presents evidences of the differential activation of CDPKs in response to elicitors from different races of<em>P. infestans</em>, revealing that these protein kinases participate in the defence response to oomycete.
publishDate 2008
dc.date.none.fl_str_mv 2008-01-30
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/submittedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str submittedVersion
dc.identifier.none.fl_str_mv https://digital.cic.gba.gob.ar/handle/11746/5606
url https://digital.cic.gba.gob.ar/handle/11746/5606
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:CIC Digital (CICBA)
instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
instacron:CICBA
reponame_str CIC Digital (CICBA)
collection CIC Digital (CICBA)
instname_str Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
instacron_str CICBA
institution CICBA
repository.name.fl_str_mv CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
repository.mail.fl_str_mv marisa.degiusti@sedici.unlp.edu.ar
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