Cloning and sequence analysis of a Phytophthora cinnamomi gene which encodes for cinnamomin, a toxin with implications in root rot of cranberry.
Identifieur interne : 002860 ( Main/Exploration ); précédent : 002859; suivant : 002861Cloning and sequence analysis of a Phytophthora cinnamomi gene which encodes for cinnamomin, a toxin with implications in root rot of cranberry.
Auteurs : B. Li [États-Unis] ; X. Qian ; F L Caruso ; B R Singh ; H K SarkarSource :
- Journal of natural toxins [ 1058-8108 ] ; 2000.
Descripteurs français
- KwdFr :
- Cadres ouverts de lecture (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Fruit (MeSH), Maladies des plantes (MeSH), Mycotoxines (génétique), Protéines (génétique), Protéines d'algue (MeSH), Protéines fongiques (génétique), Protéines inactivant les ribosomes de type 2 (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
English descriptors
- KwdEn :
- Algal Proteins (MeSH), Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), Fruit (MeSH), Fungal Proteins (genetics), Molecular Sequence Data (MeSH), Mycotoxins (genetics), Open Reading Frames (MeSH), Plant Diseases (MeSH), Proteins (genetics), Ribosome Inactivating Proteins, Type 2 (MeSH).
- MESH :
- chemical , genetics : Fungal Proteins, Mycotoxins, Proteins.
- chemical : Algal Proteins, Ribosome Inactivating Proteins, Type 2.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Fruit, Molecular Sequence Data, Open Reading Frames, Plant Diseases.
Abstract
We used a polymerase chain reaction (PCR) based cloning strategy to isolate cinnamomin genes from Phytophthora cinnamomi 8601, a pathogen responsible for cranberry root rot. Complete DNA sequence analysis of nine recombinant clones revealed two different classes of genes, each class consisting of genes with identical DNA sequences. Both classes of genes (Cin-1 and Cin-2) contained an open reading frame encoding a protein of 122 amino acid residues. The encoded proteins, named cinnamomin-1 and cinnamomin-2 (Cin-1 and Cin-2), were highly homologous to other proteins of the elicitin family and contained a 19 amino acid residue long signal peptide sequence. Both Cin-1 and Cin-2 proteins showed higher degree of sequence homology to the alpha-elicitins than beta-elicitins; moreover, a Val residue was found at position 13 of the putative mature Cin-1 and Cin-2 proteins. Because alpha-elicitins and beta-elicitins are known to contain a Val and a Lys residue, respectively, at this position, we concluded that both Cin-1 and Cin-2 genes from P. cinnamomi 8601 encode for alpha cinnamomins, Cin-1 and Cin-2.
PubMed: 10868339
Affiliations:
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Qian</name></author><author><name sortKey="Caruso, F L" sort="Caruso, F L" uniqKey="Caruso F" first="F L" last="Caruso">F L Caruso</name></author><author><name sortKey="Singh, B R" sort="Singh, B R" uniqKey="Singh B" first="B R" last="Singh">B R Singh</name></author><author><name sortKey="Sarkar, H K" sort="Sarkar, H K" uniqKey="Sarkar H" first="H K" last="Sarkar">H K Sarkar</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2000">2000</date><idno type="RBID">pubmed:10868339</idno><idno type="pmid">10868339</idno><idno type="wicri:Area/Main/Corpus">002866</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002866</idno><idno type="wicri:Area/Main/Curation">002866</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002866</idno><idno type="wicri:Area/Main/Exploration">002866</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Cloning and sequence analysis of a Phytophthora cinnamomi gene which encodes for cinnamomin, a toxin with implications in root rot of cranberry.</title><author><name sortKey="Li, B" sort="Li, B" uniqKey="Li B" first="B" last="Li">B. Li</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biology, University of Massachusetts, Dartmouth 02747, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biology, University of Massachusetts, Dartmouth 02747</wicri:regionArea><orgName type="university">Université du Massachusetts</orgName><placeName><settlement type="city">Amherst (Massachusetts)</settlement><region type="state">Massachusetts</region></placeName></affiliation></author><author><name sortKey="Qian, X" sort="Qian, X" uniqKey="Qian X" first="X" last="Qian">X. Qian</name></author><author><name sortKey="Caruso, F L" sort="Caruso, F L" uniqKey="Caruso F" first="F L" last="Caruso">F L Caruso</name></author><author><name sortKey="Singh, B R" sort="Singh, B R" uniqKey="Singh B" first="B R" last="Singh">B R Singh</name></author><author><name sortKey="Sarkar, H K" sort="Sarkar, H K" uniqKey="Sarkar H" first="H K" last="Sarkar">H K Sarkar</name></author></analytic><series><title level="j">Journal of natural toxins</title><idno type="ISSN">1058-8108</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Algal Proteins (MeSH)</term><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Fruit (MeSH)</term><term>Fungal Proteins (genetics)</term><term>Molecular Sequence Data (MeSH)</term><term>Mycotoxins (genetics)</term><term>Open Reading Frames (MeSH)</term><term>Plant Diseases (MeSH)</term><term>Proteins (genetics)</term><term>Ribosome Inactivating Proteins, Type 2 (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cadres ouverts de lecture (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Fruit (MeSH)</term><term>Maladies des plantes (MeSH)</term><term>Mycotoxines (génétique)</term><term>Protéines (génétique)</term><term>Protéines d'algue (MeSH)</term><term>Protéines fongiques (génétique)</term><term>Protéines inactivant les ribosomes de type 2 (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term><term>Mycotoxins</term><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Algal Proteins</term><term>Ribosome Inactivating Proteins, Type 2</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Mycotoxines</term><term>Protéines</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Fruit</term><term>Molecular Sequence Data</term><term>Open Reading Frames</term><term>Plant Diseases</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cadres ouverts de lecture</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Fruit</term><term>Maladies des plantes</term><term>Protéines d'algue</term><term>Protéines inactivant les ribosomes de type 2</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We used a polymerase chain reaction (PCR) based cloning strategy to isolate cinnamomin genes from Phytophthora cinnamomi 8601, a pathogen responsible for cranberry root rot. Complete DNA sequence analysis of nine recombinant clones revealed two different classes of genes, each class consisting of genes with identical DNA sequences. Both classes of genes (Cin-1 and Cin-2) contained an open reading frame encoding a protein of 122 amino acid residues. The encoded proteins, named cinnamomin-1 and cinnamomin-2 (Cin-1 and Cin-2), were highly homologous to other proteins of the elicitin family and contained a 19 amino acid residue long signal peptide sequence. Both Cin-1 and Cin-2 proteins showed higher degree of sequence homology to the alpha-elicitins than beta-elicitins; moreover, a Val residue was found at position 13 of the putative mature Cin-1 and Cin-2 proteins. Because alpha-elicitins and beta-elicitins are known to contain a Val and a Lys residue, respectively, at this position, we concluded that both Cin-1 and Cin-2 genes from P. cinnamomi 8601 encode for alpha cinnamomins, Cin-1 and Cin-2.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10868339</PMID><DateCompleted><Year>2000</Year><Month>12</Month><Day>05</Day></DateCompleted><DateRevised><Year>2012</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1058-8108</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>2</Issue><PubDate><Year>2000</Year><Month>May</Month></PubDate></JournalIssue><Title>Journal of natural toxins</Title><ISOAbbreviation>J Nat Toxins</ISOAbbreviation></Journal><ArticleTitle>Cloning and sequence analysis of a Phytophthora cinnamomi gene which encodes for cinnamomin, a toxin with implications in root rot of cranberry.</ArticleTitle><Pagination><MedlinePgn>113-23</MedlinePgn></Pagination><Abstract><AbstractText>We used a polymerase chain reaction (PCR) based cloning strategy to isolate cinnamomin genes from Phytophthora cinnamomi 8601, a pathogen responsible for cranberry root rot. Complete DNA sequence analysis of nine recombinant clones revealed two different classes of genes, each class consisting of genes with identical DNA sequences. Both classes of genes (Cin-1 and Cin-2) contained an open reading frame encoding a protein of 122 amino acid residues. The encoded proteins, named cinnamomin-1 and cinnamomin-2 (Cin-1 and Cin-2), were highly homologous to other proteins of the elicitin family and contained a 19 amino acid residue long signal peptide sequence. Both Cin-1 and Cin-2 proteins showed higher degree of sequence homology to the alpha-elicitins than beta-elicitins; moreover, a Val residue was found at position 13 of the putative mature Cin-1 and Cin-2 proteins. Because alpha-elicitins and beta-elicitins are known to contain a Val and a Lys residue, respectively, at this position, we concluded that both Cin-1 and Cin-2 genes from P. cinnamomi 8601 encode for alpha cinnamomins, Cin-1 and Cin-2.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>B</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Massachusetts, Dartmouth 02747, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Qian</LastName><ForeName>X</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Caruso</LastName><ForeName>F L</ForeName><Initials>FL</Initials></Author><Author ValidYN="Y"><LastName>Singh</LastName><ForeName>B R</ForeName><Initials>BR</Initials></Author><Author ValidYN="Y"><LastName>Sarkar</LastName><ForeName>H K</ForeName><Initials>HK</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Nat Toxins</MedlineTA><NlmUniqueID>9208016</NlmUniqueID><ISSNLinking>1058-8108</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020418">Algal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009183">Mycotoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054790">Ribosome Inactivating Proteins, Type 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>115742-69-3</RegistryNumber><NameOfSubstance UI="C061930">cinnamomin, Phytophthora cinnamomi</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020418" MajorTopicYN="N">Algal Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005638" MajorTopicYN="N">Fruit</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009183" MajorTopicYN="N">Mycotoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016366" MajorTopicYN="N">Open Reading Frames</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="Y">Plant Diseases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054790" MajorTopicYN="N">Ribosome Inactivating Proteins, Type 2</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>6</Month><Day>27</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>2</Month><Day>28</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>6</Month><Day>27</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10868339</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Massachusetts</li></region><settlement><li>Amherst (Massachusetts)</li></settlement><orgName><li>Université du Massachusetts</li></orgName></list><tree><noCountry><name sortKey="Caruso, F L" sort="Caruso, F L" uniqKey="Caruso F" first="F L" last="Caruso">F L Caruso</name><name sortKey="Qian, X" sort="Qian, X" uniqKey="Qian X" first="X" last="Qian">X. Qian</name><name sortKey="Sarkar, H K" sort="Sarkar, H K" uniqKey="Sarkar H" first="H K" last="Sarkar">H K Sarkar</name><name sortKey="Singh, B R" sort="Singh, B R" uniqKey="Singh B" first="B R" last="Singh">B R Singh</name></noCountry><country name="États-Unis"><region name="Massachusetts"><name sortKey="Li, B" sort="Li, B" uniqKey="Li B" first="B" last="Li">B. Li</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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