Cloning and characterization of a theta class glutathione transferase from the potato pathogen Phytophthora infestans.
Identifieur interne : 002107 ( Main/Corpus ); précédent : 002106; suivant : 002108Cloning and characterization of a theta class glutathione transferase from the potato pathogen Phytophthora infestans.
Auteurs : David Bryant ; Ian Cummins ; David P. Dixon ; Robert EdwardsSource :
- Phytochemistry [ 0031-9422 ] ; 2006.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Cloning, Molecular (MeSH), Conserved Sequence (MeSH), Gene Expression (MeSH), Glutathione Transferase (chemistry), Glutathione Transferase (classification), Glutathione Transferase (genetics), Glutathione Transferase (metabolism), Humans (MeSH), Linoleic Acid (chemistry), Linoleic Acid (metabolism), Molecular Sequence Data (MeSH), Phylogeny (MeSH), Phytophthora (enzymology), Phytophthora (genetics), Plant Diseases (MeSH), Sequence Alignment (MeSH), Solanum tuberosum (microbiology).
- MESH :
- chemical , chemistry : Glutathione Transferase, Linoleic Acid.
- chemical , classification : Glutathione Transferase.
- chemical , genetics : Glutathione Transferase.
- chemical , metabolism : Glutathione Transferase, Linoleic Acid.
- enzymology : Phytophthora.
- genetics : Phytophthora.
- microbiology : Solanum tuberosum.
- Amino Acid Sequence, Cloning, Molecular, Conserved Sequence, Gene Expression, Humans, Molecular Sequence Data, Phylogeny, Plant Diseases, Sequence Alignment.
Abstract
A glutathione transferase (GST) related to the theta (T) class of enzymes found in plants and animals has been cloned from the potato pathogen Phytophthora infestans. The cDNA encoded a 25kDa polypeptide termed PiGSTT1 which was expressed in E. coli as the native protein. The purified recombinant enzyme behaved as a dimer (PiGSTT1-1) and while being unable to catalyse the glutathione conjugation of 1-chloro-2,4-dintrobenzene, was highly active as a glutathione peroxidase with organic hydroperoxide substrates. In addition to reducing the synthetic substrate cumene hydroperoxide, PiGSTT1-1 was shown to be highly active toward 9(S)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid=9(S)-HPOT, which is formed in potato plants during infection by P. infestans as a precursor of the antifungal oxylipin colnelenic acid. An antiserum was raised to PiGSTT1-1 and used to demonstrate that the respective enzyme was abundantly expressed in P. infestans both cultured on pea agar and during the infection of potato plants.
DOI: 10.1016/j.phytochem.2006.05.012
PubMed: 16797619
Links to Exploration step
pubmed:16797619Le document en format XML
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Dixon</name></author><author><name sortKey="Edwards, Robert" sort="Edwards, Robert" uniqKey="Edwards R" first="Robert" last="Edwards">Robert Edwards</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16797619</idno><idno type="pmid">16797619</idno><idno type="doi">10.1016/j.phytochem.2006.05.012</idno><idno type="wicri:Area/Main/Corpus">002107</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002107</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Cloning and characterization of a theta class glutathione transferase from the potato pathogen Phytophthora infestans.</title><author><name sortKey="Bryant, David" sort="Bryant, David" uniqKey="Bryant D" first="David" last="Bryant">David Bryant</name><affiliation><nlm:affiliation>School of Biological and Biomedical Sciences, Crop Protection Group, Durham University, South Road, Durham DH1 3LE, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Cummins, Ian" sort="Cummins, Ian" uniqKey="Cummins I" first="Ian" last="Cummins">Ian Cummins</name></author><author><name sortKey="Dixon, David P" sort="Dixon, David P" uniqKey="Dixon D" first="David P" last="Dixon">David P. Dixon</name></author><author><name sortKey="Edwards, Robert" sort="Edwards, Robert" uniqKey="Edwards R" first="Robert" last="Edwards">Robert Edwards</name></author></analytic><series><title level="j">Phytochemistry</title><idno type="ISSN">0031-9422</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Conserved Sequence (MeSH)</term><term>Gene Expression (MeSH)</term><term>Glutathione Transferase (chemistry)</term><term>Glutathione Transferase (classification)</term><term>Glutathione Transferase (genetics)</term><term>Glutathione Transferase (metabolism)</term><term>Humans (MeSH)</term><term>Linoleic Acid (chemistry)</term><term>Linoleic Acid (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Phylogeny (MeSH)</term><term>Phytophthora (enzymology)</term><term>Phytophthora (genetics)</term><term>Plant Diseases (MeSH)</term><term>Sequence Alignment (MeSH)</term><term>Solanum tuberosum (microbiology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutathione Transferase</term><term>Linoleic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione Transferase</term><term>Linoleic Acid</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phytophthora</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phytophthora</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cloning, Molecular</term><term>Conserved Sequence</term><term>Gene Expression</term><term>Humans</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Plant Diseases</term><term>Sequence Alignment</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A glutathione transferase (GST) related to the theta (T) class of enzymes found in plants and animals has been cloned from the potato pathogen Phytophthora infestans. The cDNA encoded a 25kDa polypeptide termed PiGSTT1 which was expressed in E. coli as the native protein. The purified recombinant enzyme behaved as a dimer (PiGSTT1-1) and while being unable to catalyse the glutathione conjugation of 1-chloro-2,4-dintrobenzene, was highly active as a glutathione peroxidase with organic hydroperoxide substrates. In addition to reducing the synthetic substrate cumene hydroperoxide, PiGSTT1-1 was shown to be highly active toward 9(S)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid=9(S)-HPOT, which is formed in potato plants during infection by P. infestans as a precursor of the antifungal oxylipin colnelenic acid. An antiserum was raised to PiGSTT1-1 and used to demonstrate that the respective enzyme was abundantly expressed in P. infestans both cultured on pea agar and during the infection of potato plants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16797619</PMID><DateCompleted><Year>2006</Year><Month>11</Month><Day>13</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0031-9422</ISSN><JournalIssue CitedMedium="Print"><Volume>67</Volume><Issue>14</Issue><PubDate><Year>2006</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Phytochemistry</Title><ISOAbbreviation>Phytochemistry</ISOAbbreviation></Journal><ArticleTitle>Cloning and characterization of a theta class glutathione transferase from the potato pathogen Phytophthora infestans.</ArticleTitle><Pagination><MedlinePgn>1427-34</MedlinePgn></Pagination><Abstract><AbstractText>A glutathione transferase (GST) related to the theta (T) class of enzymes found in plants and animals has been cloned from the potato pathogen Phytophthora infestans. The cDNA encoded a 25kDa polypeptide termed PiGSTT1 which was expressed in E. coli as the native protein. The purified recombinant enzyme behaved as a dimer (PiGSTT1-1) and while being unable to catalyse the glutathione conjugation of 1-chloro-2,4-dintrobenzene, was highly active as a glutathione peroxidase with organic hydroperoxide substrates. In addition to reducing the synthetic substrate cumene hydroperoxide, PiGSTT1-1 was shown to be highly active toward 9(S)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid=9(S)-HPOT, which is formed in potato plants during infection by P. infestans as a precursor of the antifungal oxylipin colnelenic acid. An antiserum was raised to PiGSTT1-1 and used to demonstrate that the respective enzyme was abundantly expressed in P. infestans both cultured on pea agar and during the infection of potato plants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bryant</LastName><ForeName>David</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>School of Biological and Biomedical Sciences, Crop Protection Group, Durham University, South Road, Durham DH1 3LE, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cummins</LastName><ForeName>Ian</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Dixon</LastName><ForeName>David P</ForeName><Initials>DP</Initials></Author><Author ValidYN="Y"><LastName>Edwards</LastName><ForeName>Robert</ForeName><Initials>R</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AM261440</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>06</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Phytochemistry</MedlineTA><NlmUniqueID>0151434</NlmUniqueID><ISSNLinking>0031-9422</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>9KJL21T0QJ</RegistryNumber><NameOfSubstance UI="D019787">Linoleic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019787" MajorTopicYN="N">Linoleic Acid</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011198" MajorTopicYN="N">Solanum tuberosum</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>03</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2006</Year><Month>05</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>05</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>6</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>11</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>6</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16797619</ArticleId><ArticleId IdType="pii">S0031-9422(06)00243-3</ArticleId><ArticleId IdType="doi">10.1016/j.phytochem.2006.05.012</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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