A Phytophthora infestans cystatin-like protein targets a novel tomato papain-like apoplastic protease.
Identifieur interne : 001F38 ( Main/Exploration ); précédent : 001F37; suivant : 001F39A Phytophthora infestans cystatin-like protein targets a novel tomato papain-like apoplastic protease.
Auteurs : Miaoying Tian [États-Unis] ; Joe Win ; Jing Song ; Renier Van Der Hoorn ; Esther Van Der Knaap ; Sophien KamounSource :
- Plant physiology [ 0032-0889 ] ; 2007.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Chromosomes de plante (MeSH), Cystatines (métabolisme), Cysteine endopeptidases (classification), Cysteine endopeptidases (composition chimique), Cysteine endopeptidases (métabolisme), Données de séquences moléculaires (MeSH), Inhibiteurs de la cystéine protéinase (métabolisme), Liaison génétique (MeSH), Lycopersicon esculentum (enzymologie), Lycopersicon esculentum (parasitologie), Papaïne (métabolisme), Phylogenèse (MeSH), Phytophthora (pathogénicité), Protéines d'algue (classification), Protéines d'algue (composition chimique), Protéines d'algue (métabolisme), Protéines végétales (antagonistes et inhibiteurs), Protéines végétales (métabolisme), Séquence d'acides aminés (MeSH), Étiquettes de séquences exprimées (MeSH).
- MESH :
- antagonistes et inhibiteurs : Protéines végétales.
- classification : Cysteine endopeptidases, Protéines d'algue.
- composition chimique : Cysteine endopeptidases, Protéines d'algue.
- enzymologie : Lycopersicon esculentum.
- métabolisme : Cystatines, Cysteine endopeptidases, Inhibiteurs de la cystéine protéinase, Papaïne, Protéines d'algue, Protéines végétales.
- parasitologie : Lycopersicon esculentum.
- pathogénicité : Phytophthora.
- Alignement de séquences, Chromosomes de plante, Données de séquences moléculaires, Liaison génétique, Phylogenèse, Séquence d'acides aminés, Étiquettes de séquences exprimées.
English descriptors
- KwdEn :
- Algal Proteins (chemistry), Algal Proteins (classification), Algal Proteins (metabolism), Amino Acid Sequence (MeSH), Chromosomes, Plant (MeSH), Cystatins (metabolism), Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (classification), Cysteine Endopeptidases (metabolism), Cysteine Proteinase Inhibitors (metabolism), Expressed Sequence Tags (MeSH), Genetic Linkage (MeSH), Lycopersicon esculentum (enzymology), Lycopersicon esculentum (parasitology), Molecular Sequence Data (MeSH), Papain (metabolism), Phylogeny (MeSH), Phytophthora (pathogenicity), Plant Proteins (antagonists & inhibitors), Plant Proteins (metabolism), Sequence Alignment (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Plant Proteins.
- chemical , chemistry : Algal Proteins, Cysteine Endopeptidases.
- chemical , classification : Algal Proteins, Cysteine Endopeptidases.
- chemical , metabolism : Algal Proteins, Cystatins, Cysteine Endopeptidases, Cysteine Proteinase Inhibitors, Papain, Plant Proteins.
- enzymology : Lycopersicon esculentum.
- parasitology : Lycopersicon esculentum.
- pathogenicity : Phytophthora.
- Amino Acid Sequence, Chromosomes, Plant, Expressed Sequence Tags, Genetic Linkage, Molecular Sequence Data, Phylogeny, Sequence Alignment.
Abstract
There is emerging evidence that the proteolytic machinery of plants plays important roles in defense against pathogens. The oomycete pathogen Phytophthora infestans, the agent of the devastating late blight disease of tomato (Lycopersicon esculentum) and potato (Solanum tuberosum), has evolved an arsenal of protease inhibitors to overcome the action of host proteases. Previously, we described a family of 14 Kazal-like extracellular serine protease inhibitors from P. infestans. Among these, EPI1 and EPI10 bind and inhibit the pathogenesis-related (PR) P69B subtilisin-like serine protease of tomato. Here, we describe EPIC1 to EPIC4, a new family of P. infestans secreted proteins with similarity to cystatin-like protease inhibitor domains. Among these, the epiC1 and epiC2 genes lacked orthologs in Phytophthora sojae and Phytophthora ramorum, were relatively fast-evolving within P. infestans, and were up-regulated during infection of tomato, suggesting a role during P. infestans-host interactions. Biochemical functional analyses revealed that EPIC2B interacts with and inhibits a novel papain-like extracellular cysteine protease, termed Phytophthora Inhibited Protease 1 (PIP1). Characterization of PIP1 revealed that it is a PR protein closely related to Rcr3, a tomato apoplastic cysteine protease that functions in fungal resistance. Altogether, this and earlier studies suggest that interplay between host proteases of diverse catalytic families and pathogen inhibitors is a general defense-counterdefense process in plant-pathogen interactions.
DOI: 10.1104/pp.106.090050
PubMed: 17085509
PubMed Central: PMC1761951
Affiliations:
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Song</name></author><author><name sortKey="Van Der Hoorn, Renier" sort="Van Der Hoorn, Renier" uniqKey="Van Der Hoorn R" first="Renier" last="Van Der Hoorn">Renier Van Der Hoorn</name></author><author><name sortKey="Van Der Knaap, Esther" sort="Van Der Knaap, Esther" uniqKey="Van Der Knaap E" first="Esther" last="Van Der Knaap">Esther Van Der Knaap</name></author><author><name sortKey="Kamoun, Sophien" sort="Kamoun, Sophien" uniqKey="Kamoun S" first="Sophien" last="Kamoun">Sophien Kamoun</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17085509</idno><idno type="pmid">17085509</idno><idno type="doi">10.1104/pp.106.090050</idno><idno type="pmc">PMC1761951</idno><idno type="wicri:Area/Main/Corpus">002042</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002042</idno><idno type="wicri:Area/Main/Curation">002042</idno><idno type="wicri:explorRef" 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The oomycete pathogen Phytophthora infestans, the agent of the devastating late blight disease of tomato (Lycopersicon esculentum) and potato (Solanum tuberosum), has evolved an arsenal of protease inhibitors to overcome the action of host proteases. Previously, we described a family of 14 Kazal-like extracellular serine protease inhibitors from P. infestans. Among these, EPI1 and EPI10 bind and inhibit the pathogenesis-related (PR) P69B subtilisin-like serine protease of tomato. Here, we describe EPIC1 to EPIC4, a new family of P. infestans secreted proteins with similarity to cystatin-like protease inhibitor domains. Among these, the epiC1 and epiC2 genes lacked orthologs in Phytophthora sojae and Phytophthora ramorum, were relatively fast-evolving within P. infestans, and were up-regulated during infection of tomato, suggesting a role during P. infestans-host interactions. Biochemical functional analyses revealed that EPIC2B interacts with and inhibits a novel papain-like extracellular cysteine protease, termed Phytophthora Inhibited Protease 1 (PIP1). Characterization of PIP1 revealed that it is a PR protein closely related to Rcr3, a tomato apoplastic cysteine protease that functions in fungal resistance. Altogether, this and earlier studies suggest that interplay between host proteases of diverse catalytic families and pathogen inhibitors is a general defense-counterdefense process in plant-pathogen interactions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17085509</PMID><DateCompleted><Year>2007</Year><Month>03</Month><Day>22</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0032-0889</ISSN><JournalIssue CitedMedium="Print"><Volume>143</Volume><Issue>1</Issue><PubDate><Year>2007</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>A Phytophthora infestans cystatin-like protein targets a novel tomato papain-like apoplastic protease.</ArticleTitle><Pagination><MedlinePgn>364-77</MedlinePgn></Pagination><Abstract><AbstractText>There is emerging evidence that the proteolytic machinery of plants plays important roles in defense against pathogens. The oomycete pathogen Phytophthora infestans, the agent of the devastating late blight disease of tomato (Lycopersicon esculentum) and potato (Solanum tuberosum), has evolved an arsenal of protease inhibitors to overcome the action of host proteases. Previously, we described a family of 14 Kazal-like extracellular serine protease inhibitors from P. infestans. Among these, EPI1 and EPI10 bind and inhibit the pathogenesis-related (PR) P69B subtilisin-like serine protease of tomato. Here, we describe EPIC1 to EPIC4, a new family of P. infestans secreted proteins with similarity to cystatin-like protease inhibitor domains. Among these, the epiC1 and epiC2 genes lacked orthologs in Phytophthora sojae and Phytophthora ramorum, were relatively fast-evolving within P. infestans, and were up-regulated during infection of tomato, suggesting a role during P. infestans-host interactions. Biochemical functional analyses revealed that EPIC2B interacts with and inhibits a novel papain-like extracellular cysteine protease, termed Phytophthora Inhibited Protease 1 (PIP1). Characterization of PIP1 revealed that it is a PR protein closely related to Rcr3, a tomato apoplastic cysteine protease that functions in fungal resistance. Altogether, this and earlier studies suggest that interplay between host proteases of diverse catalytic families and pathogen inhibitors is a general defense-counterdefense process in plant-pathogen interactions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tian</LastName><ForeName>Miaoying</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Plant Pathology , The Ohio State University, Ohio Agricultural Research and Development Center, Wooster, Ohio 44691, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Win</LastName><ForeName>Joe</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Song</LastName><ForeName>Jing</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>van der Hoorn</LastName><ForeName>Renier</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>van der Knaap</LastName><ForeName>Esther</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Kamoun</LastName><ForeName>Sophien</ForeName><Initials>S</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>11</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Physiol</MedlineTA><NlmUniqueID>0401224</NlmUniqueID><ISSNLinking>0032-0889</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020418">Algal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015891">Cystatins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015853">Cysteine Proteinase Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="D003546">Cysteine Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.2</RegistryNumber><NameOfSubstance UI="D010206">Papain</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020418" MajorTopicYN="N">Algal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032461" MajorTopicYN="N">Chromosomes, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015891" MajorTopicYN="N">Cystatins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015853" MajorTopicYN="N">Cysteine Proteinase Inhibitors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020224" MajorTopicYN="N">Expressed Sequence Tags</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008040" MajorTopicYN="N">Genetic Linkage</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018551" MajorTopicYN="N">Lycopersicon esculentum</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000469" MajorTopicYN="Y">parasitology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010206" MajorTopicYN="N">Papain</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName><QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>11</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>3</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>11</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17085509</ArticleId><ArticleId IdType="pii">pp.106.090050</ArticleId><ArticleId IdType="doi">10.1104/pp.106.090050</ArticleId><ArticleId IdType="pmc">PMC1761951</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Curr Genet. 2002 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Kamoun</name><name sortKey="Song, Jing" sort="Song, Jing" uniqKey="Song J" first="Jing" last="Song">Jing Song</name><name sortKey="Van Der Hoorn, Renier" sort="Van Der Hoorn, Renier" uniqKey="Van Der Hoorn R" first="Renier" last="Van Der Hoorn">Renier Van Der Hoorn</name><name sortKey="Van Der Knaap, Esther" sort="Van Der Knaap, Esther" uniqKey="Van Der Knaap E" first="Esther" last="Van Der Knaap">Esther Van Der Knaap</name><name sortKey="Win, Joe" sort="Win, Joe" uniqKey="Win J" first="Joe" last="Win">Joe Win</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Tian, Miaoying" sort="Tian, Miaoying" uniqKey="Tian M" first="Miaoying" last="Tian">Miaoying Tian</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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