Serveur d'exploration Phytophthora

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Isolation and characterization of a Solanum tuberosum subtilisin-like protein with caspase-3 activity (StSBTc-3).

Identifieur interne : 000E31 ( Main/Exploration ); précédent : 000E30; suivant : 000E32

Isolation and characterization of a Solanum tuberosum subtilisin-like protein with caspase-3 activity (StSBTc-3).

Auteurs : María Belén Fernández [Argentine] ; Gustavo Raúl Daleo [Argentine] ; María Gabriela Guevara [Argentine]

Source :

RBID : pubmed:25486023

Descripteurs français

English descriptors

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.

DOI: 10.1016/j.plaphy.2014.12.001
PubMed: 25486023


Affiliations:


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Le document en format XML

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<term>Amino Acid Sequence (MeSH)</term>
<term>Apoptosis (genetics)</term>
<term>Base Sequence (MeSH)</term>
<term>Caspase 3 (genetics)</term>
<term>Caspase 3 (metabolism)</term>
<term>Cells, Cultured (MeSH)</term>
<term>Electrophoresis, Polyacrylamide Gel (MeSH)</term>
<term>Host-Pathogen Interactions (MeSH)</term>
<term>Lycopersicon esculentum (cytology)</term>
<term>Microscopy, Fluorescence (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Molecular Weight (MeSH)</term>
<term>Phylogeny (MeSH)</term>
<term>Phytophthora infestans (physiology)</term>
<term>Plant Cells (metabolism)</term>
<term>Plant Leaves (genetics)</term>
<term>Plant Leaves (metabolism)</term>
<term>Plant Leaves (microbiology)</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Solanum tuberosum (genetics)</term>
<term>Solanum tuberosum (metabolism)</term>
<term>Solanum tuberosum (microbiology)</term>
<term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH)</term>
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<term>Subtilisin (genetics)</term>
<term>Subtilisin (metabolism)</term>
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<term>Caspase-3 (génétique)</term>
<term>Caspase-3 (métabolisme)</term>
<term>Cellules cultivées (MeSH)</term>
<term>Cellules végétales (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Feuilles de plante (génétique)</term>
<term>Feuilles de plante (microbiologie)</term>
<term>Feuilles de plante (métabolisme)</term>
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<term>Lycopersicon esculentum (cytologie)</term>
<term>Masse moléculaire (MeSH)</term>
<term>Microscopie de fluorescence (MeSH)</term>
<term>Phylogenèse (MeSH)</term>
<term>Phytophthora infestans (physiologie)</term>
<term>Protéines végétales (composition chimique)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
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<term>Solanum tuberosum (microbiologie)</term>
<term>Solanum tuberosum (métabolisme)</term>
<term>Spectrométrie de masse MALDI (MeSH)</term>
<term>Subtilisine (classification)</term>
<term>Subtilisine (génétique)</term>
<term>Subtilisine (métabolisme)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
<term>Électrophorèse sur gel de polyacrylamide (MeSH)</term>
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<term>Subtilisin</term>
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<term>Plant Proteins</term>
<term>Subtilisin</term>
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<term>Subtilisine</term>
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<term>Caspase 3</term>
<term>Plant Cells</term>
<term>Plant Leaves</term>
<term>Plant Proteins</term>
<term>Solanum tuberosum</term>
<term>Subtilisin</term>
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<term>Feuilles de plante</term>
<term>Solanum tuberosum</term>
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<term>Plant Leaves</term>
<term>Solanum tuberosum</term>
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<term>Caspase-3</term>
<term>Cellules végétales</term>
<term>Feuilles de plante</term>
<term>Protéines végétales</term>
<term>Solanum tuberosum</term>
<term>Subtilisine</term>
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<term>Base Sequence</term>
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<term>Electrophoresis, Polyacrylamide Gel</term>
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<term>Microscopy, Fluorescence</term>
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<term>Données de séquences moléculaires</term>
<term>Interactions hôte-pathogène</term>
<term>Masse moléculaire</term>
<term>Microscopie de fluorescence</term>
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<term>Spectrométrie de masse MALDI</term>
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<div type="abstract" xml:lang="en">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.</div>
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<DescriptorName UI="D020860" MajorTopicYN="N">Subtilisin</DescriptorName>
<QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM">
<Keyword MajorTopicYN="N">Apoplast</Keyword>
<Keyword MajorTopicYN="N">DEVDase</Keyword>
<Keyword MajorTopicYN="N">Plant–pathogen interaction</Keyword>
<Keyword MajorTopicYN="N">Solanum tuberosum</Keyword>
<Keyword MajorTopicYN="N">Subtilisin like protein</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData>
<History>
<PubMedPubDate PubStatus="received">
<Year>2014</Year>
<Month>08</Month>
<Day>10</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted">
<Year>2014</Year>
<Month>12</Month>
<Day>02</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez">
<Year>2014</Year>
<Month>12</Month>
<Day>9</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed">
<Year>2014</Year>
<Month>12</Month>
<Day>9</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline">
<Year>2015</Year>
<Month>9</Month>
<Day>18</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList>
<ArticleId IdType="pubmed">25486023</ArticleId>
<ArticleId IdType="pii">S0981-9428(14)00364-7</ArticleId>
<ArticleId IdType="doi">10.1016/j.plaphy.2014.12.001</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations>
<list>
<country>
<li>Argentine</li>
</country>
</list>
<tree>
<country name="Argentine">
<noRegion>
<name sortKey="Fernandez, Maria Belen" sort="Fernandez, Maria Belen" uniqKey="Fernandez M" first="María Belén" last="Fernández">María Belén Fernández</name>
</noRegion>
<name sortKey="Daleo, Gustavo Raul" sort="Daleo, Gustavo Raul" uniqKey="Daleo G" first="Gustavo Raúl" last="Daleo">Gustavo Raúl Daleo</name>
<name sortKey="Guevara, Maria Gabriela" sort="Guevara, Maria Gabriela" uniqKey="Guevara M" first="María Gabriela" last="Guevara">María Gabriela Guevara</name>
</country>
</tree>
</affiliations>
</record>

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