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dc.contributor.author
Fernández, María Belén
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dc.contributor.author
Daleo, Gustavo Raul
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dc.contributor.author
Guevara, Maria Gabriela
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dc.date.available
2017-02-22T13:37:00Z
dc.date.issued
2014-12-03
dc.identifier.citation
Fernández, María Belén; Daleo, Gustavo Raul; Guevara, Maria Gabriela; Isolation and characterization of a Solanum tuberosum subtilisin-like protein with caspase- 3 activity (StSBTc-3); Elsevier Masson; Plant Physiology And Biochemistry; 86; 03-12-2014; 137-146
dc.identifier.issn
0981-9428
dc.identifier.uri
http://hdl.handle.net/11336/13280
dc.description.abstract
Plant proteases with caspase-like enzymatic activity have been widely studied during the last decade. Previously, we have reported the presence and induction of caspase-3 like activity in the apoplast of potato leaves during Solanum tuberosum- Phytophthora infestans interaction. In this work we have purified and identified a potato extracellular protease with caspase-3 like enzymatic activity from potato leaves infected with P. infestans. Results obtained from the size exclusion chromatography show that the isolated protease is a monomeric enzyme with an estimated molecular weight of 70 kDa approximately. Purified protease was analyzed by MALDI-TOF MS, showing a 100% of sequence identity with the deduced amino acid sequence of a putative subtilisin-like protease from S. tuberosum (Solgenomics protein ID: PGSC0003DMP400018521). For this reason the isolated protease was named as StSBTc-3. This report constitutes the first evidence of isolation and identification of a plant subtilisin-like protease with caspase-3 like enzymatic activity. In order to elucidate the possible function of StSBTc-3 during plant pathogen interaction, we demonstrate that like animal caspase-3, StSBTc-3 is able to produce in vitro cytoplasm shrinkage in plant cells and to induce plant cell death. This result suggest that, StSBTc-3 could exert a caspase executer function during potato- P. infestans interaction, resulting in the restriction of the pathogen spread during plant–pathogen interaction.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Masson
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Solanum Tuberosum
dc.subject
Subtilisin Like Protein
dc.subject
Devdase
dc.subject
Apoplast
dc.subject
Plant-Pathogen Interaction
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Isolation and characterization of a Solanum tuberosum subtilisin-like protein with caspase- 3 activity (StSBTc-3)
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-02-21T14:37:34Z
dc.journal.volume
86
dc.journal.pagination
137-146
dc.journal.pais
Francia
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dc.journal.ciudad
París
dc.description.fil
Fil: Fernández, María Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales; Argentina
dc.description.fil
Fil: Daleo, Gustavo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales; Argentina
dc.description.fil
Fil: Guevara, Maria Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales; Argentina
dc.journal.title
Plant Physiology And Biochemistry
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0981942814003647
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.plaphy.2014.12.001
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