A Second Kazal-like protease inhibitor from Phytophthora infestans inhibits and interacts with the apoplastic pathogenesis-related protease P69B of tomato.
Identifieur interne : 002237 ( Main/Exploration ); précédent : 002236; suivant : 002238A Second Kazal-like protease inhibitor from Phytophthora infestans inhibits and interacts with the apoplastic pathogenesis-related protease P69B of tomato.
Auteurs : Miaoying Tian [États-Unis] ; Brett Benedetti ; Sophien KamounSource :
- Plant physiology [ 0032-0889 ] ; 2005.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Amorces ADN (MeSH), Cartographie de restriction (MeSH), Chymotrypsine (métabolisme), Données de séquences moléculaires (MeSH), Inhibiteur de la trypsine pancréatique Kazal (isolement et purification), Inhibiteur de la trypsine pancréatique Kazal (pharmacologie), Lycopersicon esculentum (microbiologie), Maladies des plantes (microbiologie), Peptide hydrolases (composition chimique), Peptide hydrolases (génétique), Peptide hydrolases (métabolisme), Phytophthora (composition chimique), Phytophthora (pathogénicité), Protéines végétales (antagonistes et inhibiteurs), Protéines végétales (composition chimique), Similitude de séquences d'acides aminés (MeSH), Subtilisines (antagonistes et inhibiteurs), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH), Trypsine (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Protéines végétales, Subtilisines.
- composition chimique : Peptide hydrolases, Phytophthora, Protéines végétales.
- génétique : Peptide hydrolases.
- isolement et purification : Inhibiteur de la trypsine pancréatique Kazal.
- microbiologie : Lycopersicon esculentum, Maladies des plantes.
- métabolisme : Chymotrypsine, Peptide hydrolases, Trypsine.
- pathogénicité : Phytophthora.
- pharmacologie : Inhibiteur de la trypsine pancréatique Kazal.
- Alignement de séquences, Amorces ADN, Cartographie de restriction, Données de séquences moléculaires, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Chymotrypsin (metabolism), DNA Primers (MeSH), Lycopersicon esculentum (microbiology), Molecular Sequence Data (MeSH), Peptide Hydrolases (chemistry), Peptide Hydrolases (genetics), Peptide Hydrolases (metabolism), Phytophthora (chemistry), Phytophthora (pathogenicity), Plant Diseases (microbiology), Plant Proteins (antagonists & inhibitors), Plant Proteins (chemistry), Restriction Mapping (MeSH), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Subtilisins (antagonists & inhibitors), Trypsin (metabolism), Trypsin Inhibitor, Kazal Pancreatic (isolation & purification), Trypsin Inhibitor, Kazal Pancreatic (pharmacology).
- MESH :
- chemical , antagonists & inhibitors : Plant Proteins, Subtilisins.
- chemical , chemistry : Peptide Hydrolases, Plant Proteins.
- chemical , genetics : Peptide Hydrolases.
- chemical , isolation & purification : Trypsin Inhibitor, Kazal Pancreatic.
- chemical , metabolism : Chymotrypsin, Peptide Hydrolases, Trypsin.
- chemistry : Phytophthora.
- microbiology : Lycopersicon esculentum, Plant Diseases.
- pathogenicity : Phytophthora.
- chemical , pharmacology : Trypsin Inhibitor, Kazal Pancreatic.
- Amino Acid Sequence, Base Sequence, DNA Primers, Molecular Sequence Data, Restriction Mapping, Sequence Alignment, Sequence Homology, Amino Acid.
Abstract
The plant apoplast forms a protease-rich environment in which proteases are integral components of the plant defense response. Plant pathogenic oomycetes, such as the potato (Solanum tuberosum) and tomato (Lycopersicon esculentum) pathogen Phytophthora infestans, secrete a diverse family of serine protease inhibitors of the Kazal family. Among these, the two-domain EPI1 protein was shown to inhibit and interact with the pathogenesis-related protein P69B subtilase of tomato and was implicated in counter-defense. Here, we describe and functionally characterize a second extracellular protease inhibitor, EPI10, from P. infestans. EPI10 contains three Kazal-like domains, one of which was predicted to be an efficient inhibitor of subtilisin A by an additivity-based sequence to reactivity algorithm (Laskowski algorithm). The epi10 gene was up-regulated during infection of tomato, suggesting a potential role during pathogenesis. Recombinant EPI10 specifically inhibited subtilisin A among the major serine proteases, and inhibited and interacted with P69B subtilase of tomato. The finding that P. infestans evolved two distinct and structurally divergent protease inhibitors to target the same plant protease suggests that inhibition of P69B could be an important infection mechanism for this pathogen.
DOI: 10.1104/pp.105.061226
PubMed: 15980196
PubMed Central: PMC1176446
Affiliations:
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séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The plant apoplast forms a protease-rich environment in which proteases are integral components of the plant defense response. Plant pathogenic oomycetes, such as the potato (Solanum tuberosum) and tomato (Lycopersicon esculentum) pathogen Phytophthora infestans, secrete a diverse family of serine protease inhibitors of the Kazal family. Among these, the two-domain EPI1 protein was shown to inhibit and interact with the pathogenesis-related protein P69B subtilase of tomato and was implicated in counter-defense. Here, we describe and functionally characterize a second extracellular protease inhibitor, EPI10, from P. infestans. EPI10 contains three Kazal-like domains, one of which was predicted to be an efficient inhibitor of subtilisin A by an additivity-based sequence to reactivity algorithm (Laskowski algorithm). The epi10 gene was up-regulated during infection of tomato, suggesting a potential role during pathogenesis. Recombinant EPI10 specifically inhibited subtilisin A among the major serine proteases, and inhibited and interacted with P69B subtilase of tomato. The finding that P. infestans evolved two distinct and structurally divergent protease inhibitors to target the same plant protease suggests that inhibition of P69B could be an important infection mechanism for this pathogen.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15980196</PMID><DateCompleted><Year>2005</Year><Month>10</Month><Day>27</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>138</Volume><Issue>3</Issue><PubDate><Year>2005</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>A Second Kazal-like protease inhibitor from Phytophthora infestans inhibits and interacts with the apoplastic pathogenesis-related protease P69B of tomato.</ArticleTitle><Pagination><MedlinePgn>1785-93</MedlinePgn></Pagination><Abstract><AbstractText>The plant apoplast forms a protease-rich environment in which proteases are integral components of the plant defense response. Plant pathogenic oomycetes, such as the potato (Solanum tuberosum) and tomato (Lycopersicon esculentum) pathogen Phytophthora infestans, secrete a diverse family of serine protease inhibitors of the Kazal family. Among these, the two-domain EPI1 protein was shown to inhibit and interact with the pathogenesis-related protein P69B subtilase of tomato and was implicated in counter-defense. Here, we describe and functionally characterize a second extracellular protease inhibitor, EPI10, from P. infestans. EPI10 contains three Kazal-like domains, one of which was predicted to be an efficient inhibitor of subtilisin A by an additivity-based sequence to reactivity algorithm (Laskowski algorithm). The epi10 gene was up-regulated during infection of tomato, suggesting a potential role during pathogenesis. Recombinant EPI10 specifically inhibited subtilisin A among the major serine proteases, and inhibited and interacted with P69B subtilase of tomato. The finding that P. infestans evolved two distinct and structurally divergent protease inhibitors to target the same plant protease suggests that inhibition of P69B could be an important infection mechanism for this pathogen.</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>Benedetti</LastName><ForeName>Brett</ForeName><Initials>B</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="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>06</Month><Day>24</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="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>50936-63-5</RegistryNumber><NameOfSubstance UI="D014359">Trypsin Inhibitor, Kazal Pancreatic</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010447">Peptide Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="D013381">Subtilisins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.1</RegistryNumber><NameOfSubstance UI="D002918">Chymotrypsin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.4</RegistryNumber><NameOfSubstance UI="D014357">Trypsin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002918" MajorTopicYN="N">Chymotrypsin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018551" MajorTopicYN="N">Lycopersicon esculentum</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010447" MajorTopicYN="N">Peptide Hydrolases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015183" MajorTopicYN="N">Restriction Mapping</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013381" MajorTopicYN="N">Subtilisins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014357" MajorTopicYN="N">Trypsin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014359" MajorTopicYN="N">Trypsin Inhibitor, Kazal 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IdType="pubmed">8055907</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Benedetti, Brett" sort="Benedetti, Brett" uniqKey="Benedetti B" first="Brett" last="Benedetti">Brett Benedetti</name><name sortKey="Kamoun, Sophien" sort="Kamoun, Sophien" uniqKey="Kamoun S" first="Sophien" last="Kamoun">Sophien Kamoun</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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