Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge

Autores
Zanetti, María Eugenia; Blanco, Flavio Antonio; Daleo, Gustavo Raul; Casalongue, Claudia
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
StMBF1 (Solanum tuberosum multiprotein bridging factor 1) is a plant member of the MBF1 family of transcriptional co-activators. Previously, it has been described as being up-regulated at the transcriptional level by fungal and abiotic stress. To understand whether StMBF1 is also regulated at the post-- translational level, in vitro as well as in vivo phosphorylation assays were performed. StMBF1 is phosphorylated under both experimental conditions and [32P] incorporation into StMBF1 increases after treatment of potato cells with hyphal cell wall components (HWC) derived from Phytophthora infestans. The StMBF1-phosphorylating activity is strongly inhibited by the calcium-chelator EGTA and partially inhibited by calmodulin antagonists. Using bacterial puri®ed StMBF1 as a substrate, a 57 kDa calcium-dependent protein kinase (p57) that is able to phosphorylate StMBF1 was detected. The StMBF1 kinase activity of p57 was higher in elicited than in non-treated cells. The role of the elicitor-dependent phosphorylation of StMBF1 is discussed
Fil: Zanetti, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Blanco, Flavio Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Daleo, Gustavo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Casalongue, Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Materia
MBF
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:11336/173034
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/173034
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challengeZanetti, María EugeniaBlanco, Flavio AntonioDaleo, Gustavo RaulCasalongue, ClaudiaMBFhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1StMBF1 (Solanum tuberosum multiprotein bridging factor 1) is a plant member of the MBF1 family of transcriptional co-activators. Previously, it has been described as being up-regulated at the transcriptional level by fungal and abiotic stress. To understand whether StMBF1 is also regulated at the post-- translational level, in vitro as well as in vivo phosphorylation assays were performed. StMBF1 is phosphorylated under both experimental conditions and [32P] incorporation into StMBF1 increases after treatment of potato cells with hyphal cell wall components (HWC) derived from Phytophthora infestans. The StMBF1-phosphorylating activity is strongly inhibited by the calcium-chelator EGTA and partially inhibited by calmodulin antagonists. Using bacterial puri®ed StMBF1 as a substrate, a 57 kDa calcium-dependent protein kinase (p57) that is able to phosphorylate StMBF1 was detected. The StMBF1 kinase activity of p57 was higher in elicited than in non-treated cells. The role of the elicitor-dependent phosphorylation of StMBF1 is discussedFil: Zanetti, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaFil: Blanco, Flavio Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaFil: Daleo, Gustavo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaFil: Casalongue, Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaOxford University Press2003-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/173034Zanetti, María Eugenia; Blanco, Flavio Antonio; Daleo, Gustavo Raul; Casalongue, Claudia; Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge; Oxford University Press; Journal of Experimental Botany; 54; 12-2003; 623-6320022-0957CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jxb/article/54/383/623/545725?login=falseinfo:eu-repo/semantics/altIdentifier/doi/10.1093/jxb/erg061info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:45:19Zoai:ri.conicet.gov.ar:11336/173034instacron: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 10:45:19.304CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge
title Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge
spellingShingle Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge
Zanetti, María Eugenia
MBF
title_short Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge
title_full Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge
title_fullStr Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge
title_full_unstemmed Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge
title_sort Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge
dc.creator.none.fl_str_mv Zanetti, María Eugenia
Blanco, Flavio Antonio
Daleo, Gustavo Raul
Casalongue, Claudia
author Zanetti, María Eugenia
author_facet Zanetti, María Eugenia
Blanco, Flavio Antonio
Daleo, Gustavo Raul
Casalongue, Claudia
author_role author
author2 Blanco, Flavio Antonio
Daleo, Gustavo Raul
Casalongue, Claudia
author2_role author
author
author
dc.subject.none.fl_str_mv MBF
topic MBF
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv StMBF1 (Solanum tuberosum multiprotein bridging factor 1) is a plant member of the MBF1 family of transcriptional co-activators. Previously, it has been described as being up-regulated at the transcriptional level by fungal and abiotic stress. To understand whether StMBF1 is also regulated at the post-- translational level, in vitro as well as in vivo phosphorylation assays were performed. StMBF1 is phosphorylated under both experimental conditions and [32P] incorporation into StMBF1 increases after treatment of potato cells with hyphal cell wall components (HWC) derived from Phytophthora infestans. The StMBF1-phosphorylating activity is strongly inhibited by the calcium-chelator EGTA and partially inhibited by calmodulin antagonists. Using bacterial puri®ed StMBF1 as a substrate, a 57 kDa calcium-dependent protein kinase (p57) that is able to phosphorylate StMBF1 was detected. The StMBF1 kinase activity of p57 was higher in elicited than in non-treated cells. The role of the elicitor-dependent phosphorylation of StMBF1 is discussed
Fil: Zanetti, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Blanco, Flavio Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Daleo, Gustavo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Casalongue, Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
description StMBF1 (Solanum tuberosum multiprotein bridging factor 1) is a plant member of the MBF1 family of transcriptional co-activators. Previously, it has been described as being up-regulated at the transcriptional level by fungal and abiotic stress. To understand whether StMBF1 is also regulated at the post-- translational level, in vitro as well as in vivo phosphorylation assays were performed. StMBF1 is phosphorylated under both experimental conditions and [32P] incorporation into StMBF1 increases after treatment of potato cells with hyphal cell wall components (HWC) derived from Phytophthora infestans. The StMBF1-phosphorylating activity is strongly inhibited by the calcium-chelator EGTA and partially inhibited by calmodulin antagonists. Using bacterial puri®ed StMBF1 as a substrate, a 57 kDa calcium-dependent protein kinase (p57) that is able to phosphorylate StMBF1 was detected. The StMBF1 kinase activity of p57 was higher in elicited than in non-treated cells. The role of the elicitor-dependent phosphorylation of StMBF1 is discussed
publishDate 2003
dc.date.none.fl_str_mv 2003-12
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/11336/173034
Zanetti, María Eugenia; Blanco, Flavio Antonio; Daleo, Gustavo Raul; Casalongue, Claudia; Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge; Oxford University Press; Journal of Experimental Botany; 54; 12-2003; 623-632
0022-0957
CONICET Digital
CONICET
url http://hdl.handle.net/11336/173034
identifier_str_mv Zanetti, María Eugenia; Blanco, Flavio Antonio; Daleo, Gustavo Raul; Casalongue, Claudia; Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge; Oxford University Press; Journal of Experimental Botany; 54; 12-2003; 623-632
0022-0957
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://academic.oup.com/jxb/article/54/383/623/545725?login=false
info:eu-repo/semantics/altIdentifier/doi/10.1093/jxb/erg061
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
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
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_ 1844614492580741120
score 13.070432

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