[Role of proteinase inhibitors in potato protection].
Identifieur interne : 002377 ( Main/Exploration ); précédent : 002376; suivant : 002378[Role of proteinase inhibitors in potato protection].
Auteurs : T A Valueva [Russie] ; T A Revina ; E L Gvozdeva ; N G Gerasimova ; O L OzeretskovskaiaSource :
- Bioorganicheskaia khimiia [ 0132-3423 ]
Descripteurs français
- KwdFr :
- Chromatographie d'affinité (MeSH), Données de séquences moléculaires (MeSH), Inhibiteurs de protéases (composition chimique), Inhibiteurs de protéases (métabolisme), Masse moléculaire (MeSH), Similitude de séquences d'acides aminés (MeSH), Solanum tuberosum (métabolisme), Séquence d'acides aminés (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Protease Inhibitors.
- chemical , metabolism : Protease Inhibitors.
- metabolism : Solanum tuberosum.
- Amino Acid Sequence, Chromatography, Affinity, Electrophoresis, Polyacrylamide Gel, Molecular Sequence Data, Molecular Weight, Sequence Homology, Amino Acid.
Abstract
Mechanical damage or infection of potatoes with Phytophthora infestans caused an accumulation of only serine protease inhibitors in exudates of potato tubers. Among them, proteins prevailed that are structurally similar to those present in healthy tubers: a 22-kDa trypsin inhibitor, a 21-kDa serine protease inhibitor consisting of two polypeptide chains, and a 8-kDa potato chymotrypsin I inhibitor produced de novo. The accumulated proteins inhibited the growth of hyphae and germination of zoospores of P. infestans. Treatment with elicitors, jasmonic and arachidonic acids, intensified the accumulation of these inhibitors in tubers in response to the wound stress, whereas salicylic acid blocked this process. These results suggest that the lipoxygenase metabolism plays a substantial role in signal transduction of the protective system of resting potato tubers.
DOI: 10.1023/a:1026053626260
PubMed: 14601405
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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sortKey="Gerasimova, N G" sort="Gerasimova, N G" uniqKey="Gerasimova N" first="N G" last="Gerasimova">N G Gerasimova</name></author><author><name sortKey="Ozeretskovskaia, O L" sort="Ozeretskovskaia, O L" uniqKey="Ozeretskovskaia O" first="O L" last="Ozeretskovskaia">O L Ozeretskovskaia</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2003">2003 Sep-Oct</date><idno type="RBID">pubmed:14601405</idno><idno type="pmid">14601405</idno><idno type="doi">10.1023/a:1026053626260</idno><idno type="wicri:Area/Main/Corpus">002459</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002459</idno><idno type="wicri:Area/Main/Curation">002459</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002459</idno><idno type="wicri:Area/Main/Exploration">002459</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">[Role of proteinase inhibitors in potato protection].</title><author><name sortKey="Valueva, T A" sort="Valueva, T A" uniqKey="Valueva T" first="T A" last="Valueva">T A Valueva</name><affiliation wicri:level="3"><nlm:affiliation>Bakh Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 119071 Russia. valueva@inbi.ras.ru</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Bakh Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Revina, T A" sort="Revina, T A" uniqKey="Revina T" first="T A" last="Revina">T A Revina</name></author><author><name sortKey="Gvozdeva, E L" sort="Gvozdeva, E L" uniqKey="Gvozdeva E" first="E L" last="Gvozdeva">E L Gvozdeva</name></author><author><name sortKey="Gerasimova, N G" sort="Gerasimova, N G" uniqKey="Gerasimova N" first="N G" last="Gerasimova">N G Gerasimova</name></author><author><name sortKey="Ozeretskovskaia, O L" sort="Ozeretskovskaia, O L" uniqKey="Ozeretskovskaia O" first="O L" last="Ozeretskovskaia">O L Ozeretskovskaia</name></author></analytic><series><title level="j">Bioorganicheskaia khimiia</title><idno type="ISSN">0132-3423</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Chromatography, Affinity (MeSH)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Molecular Weight (MeSH)</term><term>Protease Inhibitors (chemistry)</term><term>Protease Inhibitors (metabolism)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Solanum tuberosum (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chromatographie d'affinité (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Inhibiteurs de protéases (composition chimique)</term><term>Inhibiteurs de protéases (métabolisme)</term><term>Masse moléculaire (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Solanum tuberosum (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Protease Inhibitors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Protease Inhibitors</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Inhibiteurs de protéases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Inhibiteurs de protéases</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Chromatography, Affinity</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Molecular Sequence Data</term><term>Molecular Weight</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie d'affinité</term><term>Données de séquences moléculaires</term><term>Masse moléculaire</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mechanical damage or infection of potatoes with Phytophthora infestans caused an accumulation of only serine protease inhibitors in exudates of potato tubers. Among them, proteins prevailed that are structurally similar to those present in healthy tubers: a 22-kDa trypsin inhibitor, a 21-kDa serine protease inhibitor consisting of two polypeptide chains, and a 8-kDa potato chymotrypsin I inhibitor produced de novo. The accumulated proteins inhibited the growth of hyphae and germination of zoospores of P. infestans. Treatment with elicitors, jasmonic and arachidonic acids, intensified the accumulation of these inhibitors in tubers in response to the wound stress, whereas salicylic acid blocked this process. These results suggest that the lipoxygenase metabolism plays a substantial role in signal transduction of the protective system of resting potato tubers.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14601405</PMID><DateCompleted><Year>2004</Year><Month>03</Month><Day>01</Day></DateCompleted><DateRevised><Year>2019</Year><Month>10</Month><Day>26</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0132-3423</ISSN><JournalIssue CitedMedium="Print"><Volume>29</Volume><Issue>5</Issue><PubDate><MedlineDate>2003 Sep-Oct</MedlineDate></PubDate></JournalIssue><Title>Bioorganicheskaia khimiia</Title><ISOAbbreviation>Bioorg Khim</ISOAbbreviation></Journal><ArticleTitle>[Role of proteinase inhibitors in potato protection].</ArticleTitle><Pagination><MedlinePgn>499-504</MedlinePgn></Pagination><Abstract><AbstractText>Mechanical damage or infection of potatoes with Phytophthora infestans caused an accumulation of only serine protease inhibitors in exudates of potato tubers. Among them, proteins prevailed that are structurally similar to those present in healthy tubers: a 22-kDa trypsin inhibitor, a 21-kDa serine protease inhibitor consisting of two polypeptide chains, and a 8-kDa potato chymotrypsin I inhibitor produced de novo. The accumulated proteins inhibited the growth of hyphae and germination of zoospores of P. infestans. Treatment with elicitors, jasmonic and arachidonic acids, intensified the accumulation of these inhibitors in tubers in response to the wound stress, whereas salicylic acid blocked this process. These results suggest that the lipoxygenase metabolism plays a substantial role in signal transduction of the protective system of resting potato tubers.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Valueva</LastName><ForeName>T A</ForeName><Initials>TA</Initials><AffiliationInfo><Affiliation>Bakh Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 119071 Russia. valueva@inbi.ras.ru</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Revina</LastName><ForeName>T A</ForeName><Initials>TA</Initials></Author><Author ValidYN="Y"><LastName>Gvozdeva</LastName><ForeName>E L</ForeName><Initials>EL</Initials></Author><Author ValidYN="Y"><LastName>Gerasimova</LastName><ForeName>N G</ForeName><Initials>NG</Initials></Author><Author ValidYN="Y"><LastName>Ozeretskovskaia</LastName><ForeName>O L</ForeName><Initials>OL</Initials></Author></AuthorList><Language>rus</Language><PublicationTypeList><PublicationType UI="D004740">English Abstract</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><VernacularTitle>Rol' ingibitorov proteinaz v zashchite kartofelia.</VernacularTitle></Article><MedlineJournalInfo><Country>Russia (Federation)</Country><MedlineTA>Bioorg Khim</MedlineTA><NlmUniqueID>7804941</NlmUniqueID><ISSNLinking>0132-3423</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011480">Protease Inhibitors</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002846" MajorTopicYN="N">Chromatography, Affinity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011198" MajorTopicYN="N">Solanum tuberosum</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>11</Month><Day>7</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>3</Month><Day>3</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>11</Month><Day>7</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">14601405</ArticleId><ArticleId IdType="doi">10.1023/a:1026053626260</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Russie</li></country><region><li>District fédéral central</li></region><settlement><li>Moscou</li></settlement></list><tree><noCountry><name sortKey="Gerasimova, N G" sort="Gerasimova, N G" uniqKey="Gerasimova N" first="N G" last="Gerasimova">N G Gerasimova</name><name sortKey="Gvozdeva, E L" sort="Gvozdeva, E L" uniqKey="Gvozdeva E" first="E L" last="Gvozdeva">E L Gvozdeva</name><name sortKey="Ozeretskovskaia, O L" sort="Ozeretskovskaia, O L" uniqKey="Ozeretskovskaia O" first="O L" last="Ozeretskovskaia">O L Ozeretskovskaia</name><name sortKey="Revina, T A" sort="Revina, T A" uniqKey="Revina T" first="T A" last="Revina">T A Revina</name></noCountry><country name="Russie"><region name="District fédéral central"><name sortKey="Valueva, T A" sort="Valueva, T A" uniqKey="Valueva T" first="T A" last="Valueva">T A Valueva</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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