DEVDase activity is induced in potato leaves during Phytophthora infestans infection.
Identifieur interne : 001561 ( Main/Exploration ); précédent : 001560; suivant : 001562DEVDase activity is induced in potato leaves during Phytophthora infestans infection.
Auteurs : María Belén Fernández [Argentine] ; Gustavo Raúl Daleo ; María Gabriela GuevaraSource :
- Plant physiology and biochemistry : PPB [ 1873-2690 ] ; 2012.
Descripteurs français
- KwdFr :
- Caspase-3 (métabolisme), Feuilles de plante (microbiologie), Feuilles de plante (métabolisme), Inhibiteurs de protéases (pharmacologie), Maladies des plantes (génétique), Maladies des plantes (microbiologie), Mort cellulaire (MeSH), Peptide hydrolases (métabolisme), Phytophthora infestans (MeSH), Protéases à sérine (métabolisme), Protéines végétales (génétique), Protéines végétales (métabolisme), Résistance à la maladie (génétique), Solanum tuberosum (génétique), Solanum tuberosum (microbiologie), Solanum tuberosum (métabolisme), Spécificité d'espèce (MeSH), Subtilisine (MeSH), Sélection (MeSH).
- MESH :
- génétique : Maladies des plantes, Protéines végétales, Résistance à la maladie, Solanum tuberosum.
- microbiologie : Feuilles de plante, Maladies des plantes, Solanum tuberosum.
- métabolisme : Caspase-3, Feuilles de plante, Peptide hydrolases, Protéases à sérine, Protéines végétales, Solanum tuberosum.
- pharmacologie : Inhibiteurs de protéases.
- Mort cellulaire, Phytophthora infestans, Spécificité d'espèce, Subtilisine, Sélection.
English descriptors
- KwdEn :
- Breeding (MeSH), Caspase 3 (metabolism), Cell Death (MeSH), Disease Resistance (genetics), Peptide Hydrolases (metabolism), Phytophthora infestans (MeSH), Plant Diseases (genetics), Plant Diseases (microbiology), Plant Leaves (metabolism), Plant Leaves (microbiology), Plant Proteins (genetics), Plant Proteins (metabolism), Protease Inhibitors (pharmacology), Serine Proteases (metabolism), Solanum tuberosum (genetics), Solanum tuberosum (metabolism), Solanum tuberosum (microbiology), Species Specificity (MeSH), Subtilisin (MeSH).
- MESH :
- chemical , genetics : Plant Proteins.
- chemical , metabolism : Caspase 3, Peptide Hydrolases, Plant Proteins, Serine Proteases.
- genetics : Disease Resistance, Plant Diseases, Solanum tuberosum.
- metabolism : Plant Leaves, Solanum tuberosum.
- microbiology : Plant Diseases, Plant Leaves, Solanum tuberosum.
- chemical , pharmacology : Protease Inhibitors.
- Breeding, Cell Death, Phytophthora infestans, Species Specificity, Subtilisin.
Abstract
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 proteases; however, this percentage increases to 100% in the apoplast. Additionally, this caspase-3-like activity is constitutively expressed in the apoplast of potato leaves. Total DEVDase activity is induced only in potato cultivars with high field resistance to P. infestans. These results show that potato caspase-3-like protease could constitute a tool in the potato defense mechanisms resulting in partial resistance, although further assays would be necessary in order to elucidate its role.
DOI: 10.1016/j.plaphy.2012.10.007
PubMed: 23127523
Affiliations:
Links toward previous steps (curation, corpus...)
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Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Caspase 3</term><term>Peptide Hydrolases</term><term>Plant Proteins</term><term>Serine Proteases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Disease Resistance</term><term>Plant Diseases</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Maladies des plantes</term><term>Protéines végétales</term><term>Résistance à la maladie</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Plant Leaves</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Feuilles de plante</term><term>Maladies des plantes</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Plant Diseases</term><term>Plant Leaves</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Caspase-3</term><term>Feuilles de plante</term><term>Peptide hydrolases</term><term>Protéases à sérine</term><term>Protéines végétales</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Inhibiteurs de protéases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Protease Inhibitors</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Breeding</term><term>Cell Death</term><term>Phytophthora infestans</term><term>Species Specificity</term><term>Subtilisin</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Mort cellulaire</term><term>Phytophthora infestans</term><term>Spécificité d'espèce</term><term>Subtilisine</term><term>Sélection</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 proteases; however, this percentage increases to 100% in the apoplast. Additionally, this caspase-3-like activity is constitutively expressed in the apoplast of potato leaves. Total DEVDase activity is induced only in potato cultivars with high field resistance to P. infestans. These results show that potato caspase-3-like protease could constitute a tool in the potato defense mechanisms resulting in partial resistance, although further assays would be necessary in order to elucidate its role.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23127523</PMID><DateCompleted><Year>2013</Year><Month>05</Month><Day>30</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-2690</ISSN><JournalIssue CitedMedium="Internet"><Volume>61</Volume><PubDate><Year>2012</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Plant physiology and biochemistry : PPB</Title><ISOAbbreviation>Plant Physiol Biochem</ISOAbbreviation></Journal><ArticleTitle>DEVDase activity is induced in potato leaves during Phytophthora infestans infection.</ArticleTitle><Pagination><MedlinePgn>197-203</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.plaphy.2012.10.007</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0981-9428(12)00277-X</ELocationID><Abstract><AbstractText>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 proteases; however, this percentage increases to 100% in the apoplast. Additionally, this caspase-3-like activity is constitutively expressed in the apoplast of potato leaves. Total DEVDase activity is induced only in potato cultivars with high field resistance to P. infestans. These results show that potato caspase-3-like protease could constitute a tool in the potato defense mechanisms resulting in partial resistance, although further assays would be necessary in order to elucidate its role.</AbstractText><CopyrightInformation>Copyright © 2012 Elsevier Masson SAS. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fernández</LastName><ForeName>María Belén</ForeName><Initials>MB</Initials><AffiliationInfo><Affiliation>Instituto de Investigaciones Biológicas, Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Mar del Plata, CC 1245, 7600 Mar del Plata, Argentina. mbfernan@mdp.edu.ar</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Daleo</LastName><ForeName>Gustavo Raúl</ForeName><Initials>GR</Initials></Author><Author ValidYN="Y"><LastName>Guevara</LastName><ForeName>María Gabriela</ForeName><Initials>MG</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>10</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>France</Country><MedlineTA>Plant Physiol Biochem</MedlineTA><NlmUniqueID>9882449</NlmUniqueID><ISSNLinking>0981-9428</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011480">Protease Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010447">Peptide Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D057057">Serine Proteases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.62</RegistryNumber><NameOfSubstance UI="D020860">Subtilisin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="D053148">Caspase 3</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.99.-</RegistryNumber><NameOfSubstance UI="C108711">DEVDase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001947" MajorTopicYN="N">Breeding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053148" MajorTopicYN="N">Caspase 3</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016923" MajorTopicYN="N">Cell Death</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D060467" MajorTopicYN="Y">Disease Resistance</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010447" MajorTopicYN="N">Peptide Hydrolases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055750" MajorTopicYN="Y">Phytophthora infestans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018515" MajorTopicYN="N">Plant Leaves</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057057" MajorTopicYN="N">Serine Proteases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011198" MajorTopicYN="N">Solanum tuberosum</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013045" MajorTopicYN="N">Species Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020860" MajorTopicYN="N">Subtilisin</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>05</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>10</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>11</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>11</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>6</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23127523</ArticleId><ArticleId IdType="pii">S0981-9428(12)00277-X</ArticleId><ArticleId IdType="doi">10.1016/j.plaphy.2012.10.007</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Argentine</li></country></list><tree><noCountry><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></noCountry><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></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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