DEVDase activity is induced in potato leaves during Phytophthora infestans infection.
- Autores
- Fernández, M.B.; Daleo, Gustavo Raúl; Guevara, M.G.
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión enviada
- Descripción
- Programmed cell death (PCD) occurs in plants, animals and several branches of unicellular eukaryotes as a part of developmental and/or defense processes. Caspase proteases are universal mediators of animal apoptosis, a type of PCD. In plants, there are not animal caspase homologs; therefore, the characterization of caspase-like activities is of considerable importance to our understanding of PCD in plants. Here we report for the first time the involvement of caspase-3-like activity in the resistance mechanism of potato to Phytophthora infestans infection. We showed that disease development in infected potato leaves is dependent of caspase-3-like activity. Unlike plant DEVDases previously reported, this DEVDase activity was sensitive to the serine protease inhibitor PMSF. As reported for other subtilisin- like proteases with caspase activity, potato DEVDase activity was mainly localized in the apoplast. We demonstrated that in total protein extract DEVDase activity accounts for a 60% of serine prot
- Materia
-
Bioquímica y Biología Molecular
DEVDase
Plant caspases
Potato
P. infestans
Apoplastic proteins - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-nd/4.0/
- Repositorio
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- Institución
- Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
- OAI Identificador
- oai:digital.cic.gba.gob.ar:11746/5523
Ver los metadatos del registro completo
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DEVDase activity is induced in potato leaves during Phytophthora infestans infection.Fernández, M.B.Daleo, Gustavo RaúlGuevara, M.G.Bioquímica y Biología MolecularDEVDasePlant caspasesPotatoP. infestansApoplastic proteinsProgrammed cell death (PCD) occurs in plants, animals and several branches of unicellular eukaryotes as a part of developmental and/or defense processes. Caspase proteases are universal mediators of animal apoptosis, a type of PCD. In plants, there are not animal caspase homologs; therefore, the characterization of caspase-like activities is of considerable importance to our understanding of PCD in plants. Here we report for the first time the involvement of caspase-3-like activity in the resistance mechanism of potato to Phytophthora infestans infection. We showed that disease development in infected potato leaves is dependent of caspase-3-like activity. Unlike plant DEVDases previously reported, this DEVDase activity was sensitive to the serine protease inhibitor PMSF. As reported for other subtilisin- like proteases with caspase activity, potato DEVDase activity was mainly localized in the apoplast. We demonstrated that in total protein extract DEVDase activity accounts for a 60% of serine prot2012-10-12info: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/11746/5523enginfo: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:CICBA2025-11-06T09:35:31Zoai:digital.cic.gba.gob.ar:11746/5523Institucionalhttp://digital.cic.gba.gob.arOrganismo científico-tecnológicoNo correspondehttp://digital.cic.gba.gob.ar/oai/snrdmarisa.degiusti@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:94412025-11-06 09:35:33.698CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Airesfalse |
| dc.title.none.fl_str_mv |
DEVDase activity is induced in potato leaves during Phytophthora infestans infection. |
| title |
DEVDase activity is induced in potato leaves during Phytophthora infestans infection. |
| spellingShingle |
DEVDase activity is induced in potato leaves during Phytophthora infestans infection. Fernández, M.B. Bioquímica y Biología Molecular DEVDase Plant caspases Potato P. infestans Apoplastic proteins |
| title_short |
DEVDase activity is induced in potato leaves during Phytophthora infestans infection. |
| title_full |
DEVDase activity is induced in potato leaves during Phytophthora infestans infection. |
| title_fullStr |
DEVDase activity is induced in potato leaves during Phytophthora infestans infection. |
| title_full_unstemmed |
DEVDase activity is induced in potato leaves during Phytophthora infestans infection. |
| title_sort |
DEVDase activity is induced in potato leaves during Phytophthora infestans infection. |
| dc.creator.none.fl_str_mv |
Fernández, M.B. Daleo, Gustavo Raúl Guevara, M.G. |
| author |
Fernández, M.B. |
| author_facet |
Fernández, M.B. Daleo, Gustavo Raúl Guevara, M.G. |
| author_role |
author |
| author2 |
Daleo, Gustavo Raúl Guevara, M.G. |
| author2_role |
author author |
| dc.subject.none.fl_str_mv |
Bioquímica y Biología Molecular DEVDase Plant caspases Potato P. infestans Apoplastic proteins |
| topic |
Bioquímica y Biología Molecular DEVDase Plant caspases Potato P. infestans Apoplastic proteins |
| dc.description.none.fl_txt_mv |
Programmed cell death (PCD) occurs in plants, animals and several branches of unicellular eukaryotes as a part of developmental and/or defense processes. Caspase proteases are universal mediators of animal apoptosis, a type of PCD. In plants, there are not animal caspase homologs; therefore, the characterization of caspase-like activities is of considerable importance to our understanding of PCD in plants. Here we report for the first time the involvement of caspase-3-like activity in the resistance mechanism of potato to Phytophthora infestans infection. We showed that disease development in infected potato leaves is dependent of caspase-3-like activity. Unlike plant DEVDases previously reported, this DEVDase activity was sensitive to the serine protease inhibitor PMSF. As reported for other subtilisin- like proteases with caspase activity, potato DEVDase activity was mainly localized in the apoplast. We demonstrated that in total protein extract DEVDase activity accounts for a 60% of serine prot |
| description |
Programmed cell death (PCD) occurs in plants, animals and several branches of unicellular eukaryotes as a part of developmental and/or defense processes. Caspase proteases are universal mediators of animal apoptosis, a type of PCD. In plants, there are not animal caspase homologs; therefore, the characterization of caspase-like activities is of considerable importance to our understanding of PCD in plants. Here we report for the first time the involvement of caspase-3-like activity in the resistance mechanism of potato to Phytophthora infestans infection. We showed that disease development in infected potato leaves is dependent of caspase-3-like activity. Unlike plant DEVDases previously reported, this DEVDase activity was sensitive to the serine protease inhibitor PMSF. As reported for other subtilisin- like proteases with caspase activity, potato DEVDase activity was mainly localized in the apoplast. We demonstrated that in total protein extract DEVDase activity accounts for a 60% of serine prot |
| publishDate |
2012 |
| dc.date.none.fl_str_mv |
2012-10-12 |
| 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 |
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article |
| status_str |
submittedVersion |
| dc.identifier.none.fl_str_mv |
https://digital.cic.gba.gob.ar/handle/11746/5523 |
| url |
https://digital.cic.gba.gob.ar/handle/11746/5523 |
| 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/ |
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openAccess |
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http://creativecommons.org/licenses/by-nc-nd/4.0/ |
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application/pdf |
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Comisión de Investigaciones Científicas de la Provincia de Buenos Aires |
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CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Aires |
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marisa.degiusti@sedici.unlp.edu.ar |
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