The pipg1 gene of the oomycete Phytophthora infestans encodes a fungal-like endopolygalacturonase.
Identifieur interne : 002695 ( Main/Corpus ); précédent : 002694; suivant : 002696The pipg1 gene of the oomycete Phytophthora infestans encodes a fungal-like endopolygalacturonase.
Auteurs : Trudy A. Torto ; Laura Rauser ; Sophien KamounSource :
- Current genetics [ 0172-8083 ] ; 2002.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Fungal Proteins (chemistry), Molecular Sequence Data (MeSH), Phylogeny (MeSH), Phytophthora (enzymology), Phytophthora (genetics), Plant Diseases (microbiology), Polygalacturonase (chemistry), Polygalacturonase (genetics), Sequence Homology, Amino Acid (MeSH), Solanum tuberosum (microbiology).
- MESH :
- chemical , chemistry : Fungal Proteins, Polygalacturonase.
- enzymology : Phytophthora.
- genetics : Phytophthora, Polygalacturonase.
- microbiology : Plant Diseases, Solanum tuberosum.
- Amino Acid Sequence, Molecular Sequence Data, Phylogeny, Sequence Homology, Amino Acid.
Abstract
Endopolygalacturonases (endoPGs) are plant cell wall-degrading enzymes that have been implicated in the invasion of plant tissue by pathogenic microbes. EndoPGs have been described from bacteria, plants, insects and numerous species of phytopathogenic fungi. In this study, we describe the first endoPG sequence from oomycetes, a unique group of eukaryotic plant pathogens that exhibit fungal-like filamentous growth but share little taxonomic affinity to fungi. The characterized gene, pipg1, was identified from the potato late-blight pathogen, Phytophthora infestans, and was predicted to encode a secreted glycoprotein with all the signature sequences of endoPGs. Pipg1 was expressed during preinfection and infection stages. Phylogenetic analysis of endoPGs indicated that pipg1 forms a unique class that is significantly more similar to fungal endoPGs than to plant or bacterial ones. This unexpected affinity between PIPG1 and fungal endoPGs contrasts with phylogenies obtained using ribosomal sequences or compiled protein sequences from mitochondrial and chromosomal genes, raising interesting questions about the evolution of these enzymes in oomycetes.
DOI: 10.1007/s00294-002-0272-4
PubMed: 11919677
Links to Exploration step
pubmed:11919677Le document en format XML
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Torto</name><affiliation><nlm:affiliation>Department of Plant Pathology, The Ohio State University, Ohio Agricultural Research and Development Center, 1680 Madison Avenue, Wooster 44691, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Rauser, Laura" sort="Rauser, Laura" uniqKey="Rauser L" first="Laura" last="Rauser">Laura Rauser</name></author><author><name sortKey="Kamoun, Sophien" sort="Kamoun, Sophien" uniqKey="Kamoun S" first="Sophien" last="Kamoun">Sophien Kamoun</name></author></analytic><series><title level="j">Current genetics</title><idno type="ISSN">0172-8083</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Fungal Proteins (chemistry)</term><term>Molecular Sequence Data (MeSH)</term><term>Phylogeny (MeSH)</term><term>Phytophthora (enzymology)</term><term>Phytophthora (genetics)</term><term>Plant Diseases (microbiology)</term><term>Polygalacturonase (chemistry)</term><term>Polygalacturonase (genetics)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Solanum tuberosum (microbiology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term><term>Polygalacturonase</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><term>Polygalacturonase</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Plant Diseases</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Sequence Homology, Amino Acid</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Endopolygalacturonases (endoPGs) are plant cell wall-degrading enzymes that have been implicated in the invasion of plant tissue by pathogenic microbes. EndoPGs have been described from bacteria, plants, insects and numerous species of phytopathogenic fungi. In this study, we describe the first endoPG sequence from oomycetes, a unique group of eukaryotic plant pathogens that exhibit fungal-like filamentous growth but share little taxonomic affinity to fungi. The characterized gene, pipg1, was identified from the potato late-blight pathogen, Phytophthora infestans, and was predicted to encode a secreted glycoprotein with all the signature sequences of endoPGs. Pipg1 was expressed during preinfection and infection stages. Phylogenetic analysis of endoPGs indicated that pipg1 forms a unique class that is significantly more similar to fungal endoPGs than to plant or bacterial ones. This unexpected affinity between PIPG1 and fungal endoPGs contrasts with phylogenies obtained using ribosomal sequences or compiled protein sequences from mitochondrial and chromosomal genes, raising interesting questions about the evolution of these enzymes in oomycetes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11919677</PMID><DateCompleted><Year>2002</Year><Month>08</Month><Day>23</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0172-8083</ISSN><JournalIssue CitedMedium="Print"><Volume>40</Volume><Issue>6</Issue><PubDate><Year>2002</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Current genetics</Title><ISOAbbreviation>Curr Genet</ISOAbbreviation></Journal><ArticleTitle>The pipg1 gene of the oomycete Phytophthora infestans encodes a fungal-like endopolygalacturonase.</ArticleTitle><Pagination><MedlinePgn>385-90</MedlinePgn></Pagination><Abstract><AbstractText>Endopolygalacturonases (endoPGs) are plant cell wall-degrading enzymes that have been implicated in the invasion of plant tissue by pathogenic microbes. EndoPGs have been described from bacteria, plants, insects and numerous species of phytopathogenic fungi. In this study, we describe the first endoPG sequence from oomycetes, a unique group of eukaryotic plant pathogens that exhibit fungal-like filamentous growth but share little taxonomic affinity to fungi. The characterized gene, pipg1, was identified from the potato late-blight pathogen, Phytophthora infestans, and was predicted to encode a secreted glycoprotein with all the signature sequences of endoPGs. Pipg1 was expressed during preinfection and infection stages. Phylogenetic analysis of endoPGs indicated that pipg1 forms a unique class that is significantly more similar to fungal endoPGs than to plant or bacterial ones. This unexpected affinity between PIPG1 and fungal endoPGs contrasts with phylogenies obtained using ribosomal sequences or compiled protein sequences from mitochondrial and chromosomal genes, raising interesting questions about the evolution of these enzymes in oomycetes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Torto</LastName><ForeName>Trudy A</ForeName><Initials>TA</Initials><AffiliationInfo><Affiliation>Department of Plant Pathology, The Ohio State University, Ohio Agricultural Research and Development Center, 1680 Madison Avenue, Wooster 44691, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rauser</LastName><ForeName>Laura</ForeName><Initials>L</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>2002</Year><Month>03</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Curr Genet</MedlineTA><NlmUniqueID>8004904</NlmUniqueID><ISSNLinking>0172-8083</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.15</RegistryNumber><NameOfSubstance UI="D011096">Polygalacturonase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</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><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011096" MajorTopicYN="N">Polygalacturonase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</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="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2001</Year><Month>10</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2001</Year><Month>12</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>3</Month><Day>29</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>8</Month><Day>24</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>3</Month><Day>29</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11919677</ArticleId><ArticleId IdType="doi">10.1007/s00294-002-0272-4</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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