Cloning and analysis of pppg1, an inducible endopolygalacturonase gene from the oomycete plant pathogen Phytophthora parasitica.
Identifieur interne : 002215 ( Main/Exploration ); précédent : 002214; suivant : 002216Cloning and analysis of pppg1, an inducible endopolygalacturonase gene from the oomycete plant pathogen Phytophthora parasitica.
Auteurs : Hao-Zhi Yan [Taïwan] ; Ruey-Fen LiouSource :
- Fungal genetics and biology : FG & B [ 1087-1845 ] ; 2005.
Descripteurs français
- KwdFr :
- Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Feuilles de plante (microbiologie), Glycosylation (MeSH), Lycopersicon esculentum (microbiologie), Maladies des plantes (microbiologie), Phylogenèse (MeSH), Phytophthora (croissance et développement), Phytophthora (enzymologie), Phytophthora (génétique), Phytophthora (pathogénicité), Polygalacturonase (composition chimique), Polygalacturonase (génétique), Polygalacturonase (métabolisme), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : Polygalacturonase, Protéines fongiques.
- croissance et développement : Phytophthora.
- enzymologie : Phytophthora.
- génétique : Phytophthora, Polygalacturonase, Protéines fongiques.
- microbiologie : Feuilles de plante, Lycopersicon esculentum, Maladies des plantes.
- métabolisme : Polygalacturonase, Protéines fongiques.
- pathogénicité : Phytophthora.
- Clonage moléculaire, Données de séquences moléculaires, Glycosylation, Phylogenèse, Régulation de l'expression des gènes fongiques, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression Regulation, Fungal (MeSH), Glycosylation (MeSH), Lycopersicon esculentum (microbiology), Molecular Sequence Data (MeSH), Phylogeny (MeSH), Phytophthora (enzymology), Phytophthora (genetics), Phytophthora (growth & development), Phytophthora (pathogenicity), Plant Diseases (microbiology), Plant Leaves (microbiology), Polygalacturonase (chemistry), Polygalacturonase (genetics), Polygalacturonase (metabolism).
- MESH :
- chemical , chemistry : Fungal Proteins, Polygalacturonase.
- chemical , genetics : Fungal Proteins, Polygalacturonase.
- chemical , metabolism : Fungal Proteins, Polygalacturonase.
- enzymology : Phytophthora.
- genetics : Phytophthora.
- growth & development : Phytophthora.
- microbiology : Lycopersicon esculentum, Plant Diseases, Plant Leaves.
- pathogenicity : Phytophthora.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Gene Expression Regulation, Fungal, Glycosylation, Molecular Sequence Data, Phylogeny.
Abstract
Phytophthora parasitica is an oomycete plant pathogen that causes severe disease in a wide variety of crops. Here, we report the isolation of a gene, named pppg1, which encodes an extracellular endopolygalacturonase in P. parasitica. Both cDNA and a genomic clone were isolated and sequenced. The pppg1 gene showed standard characteristics with respect to core promoter and intron sequences of Phytophthora. The predicted protein of pppg1 has a calculated molecular mass of 39.7 kDa and a pI value of 5.2, and contains a putative signal peptide of 20 amino acid residues on the N-terminus. The deduced amino acid sequence is highly conserved with those of other Phytophthora and fungal endopolygalacturonases. Analysis by reverse transcription followed by real-time quantitative polymerase chain reaction showed that transcription of pppg1 was repressed by glucose, but induced by pectin in the culture. Moreover, pppg1 is highly expressed during interaction of P. parasitica with the host plant, suggesting its involvement in the process of host infection. Heterologous expression of pppg1 in Pichia pastoris produced proteins with molecular mass ranging from 75 to 200 kDa, very likely due to differential glycosylation by the yeast. Deglycosylation of the recombinant protein resulted in a complete loss of the endopolygalacturonase activity.
DOI: 10.1016/j.fgb.2005.01.003
PubMed: 15749053
Affiliations:
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oomycete plant pathogen that causes severe disease in a wide variety of crops. Here, we report the isolation of a gene, named pppg1, which encodes an extracellular endopolygalacturonase in P. parasitica. Both cDNA and a genomic clone were isolated and sequenced. The pppg1 gene showed standard characteristics with respect to core promoter and intron sequences of Phytophthora. The predicted protein of pppg1 has a calculated molecular mass of 39.7 kDa and a pI value of 5.2, and contains a putative signal peptide of 20 amino acid residues on the N-terminus. The deduced amino acid sequence is highly conserved with those of other Phytophthora and fungal endopolygalacturonases. Analysis by reverse transcription followed by real-time quantitative polymerase chain reaction showed that transcription of pppg1 was repressed by glucose, but induced by pectin in the culture. Moreover, pppg1 is highly expressed during interaction of P. parasitica with the host plant, suggesting its involvement in the process of host infection. Heterologous expression of pppg1 in Pichia pastoris produced proteins with molecular mass ranging from 75 to 200 kDa, very likely due to differential glycosylation by the yeast. Deglycosylation of the recombinant protein resulted in a complete loss of the endopolygalacturonase activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15749053</PMID><DateCompleted><Year>2005</Year><Month>05</Month><Day>03</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1087-1845</ISSN><JournalIssue CitedMedium="Print"><Volume>42</Volume><Issue>4</Issue><PubDate><Year>2005</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Fungal genetics and biology : FG & B</Title><ISOAbbreviation>Fungal Genet Biol</ISOAbbreviation></Journal><ArticleTitle>Cloning and analysis of pppg1, an inducible endopolygalacturonase gene from the oomycete plant pathogen Phytophthora parasitica.</ArticleTitle><Pagination><MedlinePgn>339-50</MedlinePgn></Pagination><Abstract><AbstractText>Phytophthora parasitica is an oomycete plant pathogen that causes severe disease in a wide variety of crops. Here, we report the isolation of a gene, named pppg1, which encodes an extracellular endopolygalacturonase in P. parasitica. Both cDNA and a genomic clone were isolated and sequenced. The pppg1 gene showed standard characteristics with respect to core promoter and intron sequences of Phytophthora. The predicted protein of pppg1 has a calculated molecular mass of 39.7 kDa and a pI value of 5.2, and contains a putative signal peptide of 20 amino acid residues on the N-terminus. The deduced amino acid sequence is highly conserved with those of other Phytophthora and fungal endopolygalacturonases. Analysis by reverse transcription followed by real-time quantitative polymerase chain reaction showed that transcription of pppg1 was repressed by glucose, but induced by pectin in the culture. Moreover, pppg1 is highly expressed during interaction of P. parasitica with the host plant, suggesting its involvement in the process of host infection. Heterologous expression of pppg1 in Pichia pastoris produced proteins with molecular mass ranging from 75 to 200 kDa, very likely due to differential glycosylation by the yeast. Deglycosylation of the recombinant protein resulted in a complete loss of the endopolygalacturonase activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yan</LastName><ForeName>Hao-Zhi</ForeName><Initials>HZ</Initials><AffiliationInfo><Affiliation>Department of Plant Pathology and Microbiology, National Taiwan University, Taipei 106, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liou</LastName><ForeName>Ruey-Fen</ForeName><Initials>RF</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AY697926</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United 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MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="Y">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006031" MajorTopicYN="N">Glycosylation</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="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="N">genetics</QualifierName><QualifierName 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PubStatus="revised"><Year>2004</Year><Month>12</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2005</Year><Month>01</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>3</Month><Day>8</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>5</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>3</Month><Day>8</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15749053</ArticleId><ArticleId IdType="pii">S1087-1845(05)00005-8</ArticleId><ArticleId IdType="doi">10.1016/j.fgb.2005.01.003</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Taïwan</li></country></list><tree><noCountry><name sortKey="Liou, Ruey Fen" sort="Liou, Ruey Fen" uniqKey="Liou R" first="Ruey-Fen" last="Liou">Ruey-Fen Liou</name></noCountry><country name="Taïwan"><noRegion><name sortKey="Yan, Hao Zhi" sort="Yan, Hao Zhi" uniqKey="Yan H" first="Hao-Zhi" last="Yan">Hao-Zhi Yan</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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