Molecular cloning of a novel pathogen-inducible cDNA encoding a putative acyl-CoA synthetase from Capsicum annuum L.
Identifieur interne : 001155 ( Istex/Corpus ); précédent : 001154; suivant : 001156Molecular cloning of a novel pathogen-inducible cDNA encoding a putative acyl-CoA synthetase from Capsicum annuum L.
Auteurs : Sang Jik Lee ; Mi-Chung Suh ; Shinje Kim ; Jin-Kyung Kwon ; Minwoo Kim ; Kyung-Hee Paek ; Doil Choi ; Byung-Dong KimSource :
- Plant Molecular Biology [ 0167-4412 ] ; 2001-08-01.
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- KwdEn :
Abstract
Abstract: By means of differential display, a pool of salicylic acid (SA)-induced mRNAs were identified and subsequently their cDNAs were isolated from a cDNA library prepared from SA-induced leaf tissues of hot pepper. One of these cDNA clones, designated CaSIG4, was 1900 bp and contained an open reading frame encoding 523 amino acids with a calculated molecular mass of 56.3 kDa. The predicted amino acid sequence of CaSIG4 showed high sequence similarity to the AMP-binding protein family of both prokaryotic and eukaryotic acyl-CoA synthetases. CaSIG4 transcripts accumulated rapidly after SA treatment and in response to both incompatible and compatible interactions with Xanthomonas campestris pv. vesicatoria race 1. To investigate the cis-acting elements mediating CaSIG4 expression, the CaSIG4 5′-flanking region was isolated by inverse PCR. Database searches indicated that a potential cis-regulatory element is almost identical to the consensus core sequences ACC(A/T)ACC(A/C) which are conserved among promoters of other phenylpropanoid biosynthetic genes. The subcellular localization of the CaSIG4 protein was studied by using a soluble modified GFP gene fusion delivered into epidermal cells of onion by biolistic bombardment. The CaSIG4-smGFP fusion protein was localized to the plasma membrane. Taken together, CaSIG4 encoding a putative acyl-CoA synthetase could function as a plasma membrane-bound protein with a role in signaling in plant defense.
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DOI: 10.1023/A:1011677028605
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Korea</mods:affiliation></affiliation></author><author><name sortKey="Choi, Doil" sort="Choi, Doil" uniqKey="Choi D" first="Doil" last="Choi">Doil Choi</name><affiliation><mods:affiliation>Center for Plant Molecular Genetics and Breeding Research, Seoul National University, 103 Seodoon-dong, 441-744, Suwon, fKorea</mods:affiliation></affiliation></author><author><name sortKey="Kim, Byung Dong" sort="Kim, Byung Dong" uniqKey="Kim B" first="Byung-Dong" last="Kim">Byung-Dong Kim</name><affiliation><mods:affiliation>School of Plant Science, College of Agriculture and Life Sciences, Korea</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Plant Molecular Biology</title><title level="j" type="sub">An International Journal on Molecular Biology, Molecular Genetics and Biochemistry</title><title level="j" type="abbrev">Plant Mol Biol</title><idno type="ISSN">0167-4412</idno><idno type="eISSN">1573-5028</idno><imprint><publisher>Kluwer Academic Publishers</publisher><pubPlace>Dordrecht</pubPlace><date type="published" when="2001-08-01">2001-08-01</date><biblScope unit="volume">46</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="661">661</biblScope><biblScope unit="page" to="671">671</biblScope></imprint><idno type="ISSN">0167-4412</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0167-4412</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>AMP-binding protein</term><term>Capsicum annuum L.</term><term>acyl-CoA synthetase</term><term>mRNA differential display</term><term>salicylic acid</term><term>subcellular localization</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: By means of differential display, a pool of salicylic acid (SA)-induced mRNAs were identified and subsequently their cDNAs were isolated from a cDNA library prepared from SA-induced leaf tissues of hot pepper. One of these cDNA clones, designated CaSIG4, was 1900 bp and contained an open reading frame encoding 523 amino acids with a calculated molecular mass of 56.3 kDa. The predicted amino acid sequence of CaSIG4 showed high sequence similarity to the AMP-binding protein family of both prokaryotic and eukaryotic acyl-CoA synthetases. CaSIG4 transcripts accumulated rapidly after SA treatment and in response to both incompatible and compatible interactions with Xanthomonas campestris pv. vesicatoria race 1. To investigate the cis-acting elements mediating CaSIG4 expression, the CaSIG4 5′-flanking region was isolated by inverse PCR. Database searches indicated that a potential cis-regulatory element is almost identical to the consensus core sequences ACC(A/T)ACC(A/C) which are conserved among promoters of other phenylpropanoid biosynthetic genes. The subcellular localization of the CaSIG4 protein was studied by using a soluble modified GFP gene fusion delivered into epidermal cells of onion by biolistic bombardment. The CaSIG4-smGFP fusion protein was localized to the plasma membrane. Taken together, CaSIG4 encoding a putative acyl-CoA synthetase could function as a plasma membrane-bound protein with a role in signaling in plant defense.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>Sang Jik Lee</name><affiliations><json:string>School of Plant Science, College of Agriculture and Life Sciences, Korea</json:string></affiliations></json:item><json:item><name>Mi-Chung Suh</name><affiliations><json:string>Plant Cell Biotechnology Laboratory, Korea Research Institute of Bioscience and Biotechnology, 305-600, Taejon, fKorea</json:string></affiliations></json:item><json:item><name>Shinje Kim</name><affiliations><json:string>Center for Plant Molecular Genetics and Breeding Research, Seoul National University, 103 Seodoon-dong, 441-744, Suwon, fKorea</json:string></affiliations></json:item><json:item><name>Jin-Kyung Kwon</name><affiliations><json:string>School of Plant Science, College of Agriculture and Life Sciences, Korea</json:string></affiliations></json:item><json:item><name>Minwoo Kim</name><affiliations><json:string>School of Plant Science, College of Agriculture and Life Sciences, Korea</json:string></affiliations></json:item><json:item><name>Kyung-Hee Paek</name><affiliations><json:string>Plant Molecular Biology and Genetics Laboratory, Graduate School of Biotechnology, Korea University, 136-701, Seoul, Korea</json:string></affiliations></json:item><json:item><name>Doil Choi</name><affiliations><json:string>Center for Plant Molecular Genetics and Breeding Research, Seoul National University, 103 Seodoon-dong, 441-744, Suwon, fKorea</json:string></affiliations></json:item><json:item><name>Byung-Dong Kim</name><affiliations><json:string>School of Plant Science, College of Agriculture and Life Sciences, Korea</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>acyl-CoA synthetase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>AMP-binding protein</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Capsicum annuum L.</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>mRNA differential display</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>salicylic acid</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>subcellular localization</value></json:item></subject><articleId><json:string>354101</json:string><json:string>Art3</json:string></articleId><arkIstex>ark:/67375/VQC-82XR3V3D-V</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Abstract: By means of differential display, a pool of salicylic acid (SA)-induced mRNAs were identified and subsequently their cDNAs were isolated from a cDNA library prepared from SA-induced leaf tissues of hot pepper. One of these cDNA clones, designated CaSIG4, was 1900 bp and contained an open reading frame encoding 523 amino acids with a calculated molecular mass of 56.3 kDa. The predicted amino acid sequence of CaSIG4 showed high sequence similarity to the AMP-binding protein family of both prokaryotic and eukaryotic acyl-CoA synthetases. CaSIG4 transcripts accumulated rapidly after SA treatment and in response to both incompatible and compatible interactions with Xanthomonas campestris pv. vesicatoria race 1. To investigate the cis-acting elements mediating CaSIG4 expression, the CaSIG4 5′-flanking region was isolated by inverse PCR. Database searches indicated that a potential cis-regulatory element is almost identical to the consensus core sequences ACC(A/T)ACC(A/C) which are conserved among promoters of other phenylpropanoid biosynthetic genes. The subcellular localization of the CaSIG4 protein was studied by using a soluble modified GFP gene fusion delivered into epidermal cells of onion by biolistic bombardment. The CaSIG4-smGFP fusion protein was localized to the plasma membrane. 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One of these cDNA clones, designated CaSIG4, was 1900 bp and contained an open reading frame encoding 523 amino acids with a calculated molecular mass of 56.3 kDa. The predicted amino acid sequence of CaSIG4 showed high sequence similarity to the AMP-binding protein family of both prokaryotic and eukaryotic acyl-CoA synthetases. CaSIG4 transcripts accumulated rapidly after SA treatment and in response to both incompatible and compatible interactions with Xanthomonas campestris pv. vesicatoria race 1. To investigate the cis-acting elements mediating CaSIG4 expression, the CaSIG4 5′-flanking region was isolated by inverse PCR. Database searches indicated that a potential cis-regulatory element is almost identical to the consensus core sequences ACC(A/T)ACC(A/C) which are conserved among promoters of other phenylpropanoid biosynthetic genes. The subcellular localization of the CaSIG4 protein was studied by using a soluble modified GFP gene fusion delivered into epidermal cells of onion by biolistic bombardment. The CaSIG4-smGFP fusion protein was localized to the plasma membrane. Taken together, CaSIG4 encoding a putative acyl-CoA synthetase could function as a plasma membrane-bound protein with a role in signaling in plant defense.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><item><term>acyl-CoA synthetase</term></item><item><term>AMP-binding protein</term></item><item><term>Capsicum annuum L.</term></item><item><term>mRNA differential display</term></item><item><term>salicylic acid</term></item><item><term>subcellular localization</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>Life Sciences</head><item><term>Biochemistry, general</term></item><item><term>Plant Sciences</term></item><item><term>Plant Pathology</term></item></list></keywords></textClass></profileDesc><revisionDesc><change 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Molecular Biology</JournalTitle><JournalSubTitle>An International Journal on Molecular Biology, Molecular Genetics and Biochemistry</JournalSubTitle><JournalAbbreviatedTitle>Plant Mol Biol</JournalAbbreviatedTitle><JournalSubjectGroup><JournalSubject Type="Primary">Life Sciences</JournalSubject><JournalSubject Type="Secondary">Biochemistry, general</JournalSubject><JournalSubject Type="Secondary">Plant Sciences</JournalSubject><JournalSubject Type="Secondary">Plant Pathology</JournalSubject></JournalSubjectGroup></JournalInfo><Volume><VolumeInfo VolumeType="Regular" TocLevels="0"><VolumeIDStart>46</VolumeIDStart><VolumeIDEnd>46</VolumeIDEnd><VolumeIssueCount>6</VolumeIssueCount></VolumeInfo><Issue IssueType="Regular"><IssueInfo TocLevels="0"><IssueIDStart>6</IssueIDStart><IssueIDEnd>6</IssueIDEnd><IssueArticleCount>13</IssueArticleCount><IssueHistory><CoverDate><Year>2001</Year><Month>8</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Kluwer Academic Publishers</CopyrightHolderName><CopyrightYear>2001</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art3"><ArticleInfo Language="En" ArticleType="OriginalPaper" NumberingStyle="Unnumbered" TocLevels="0" ContainsESM="No"><ArticleID>354101</ArticleID><ArticleDOI>10.1023/A:1011677028605</ArticleDOI><ArticleSequenceNumber>3</ArticleSequenceNumber><ArticleTitle Language="En">Molecular cloning of a novel pathogen-inducible cDNA encoding a putative acyl-CoA synthetase from Capsicum annuum L.</ArticleTitle><ArticleFirstPage>661</ArticleFirstPage><ArticleLastPage>671</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2004</Year><Month>10</Month><Day>3</Day></RegistrationDate></ArticleHistory><ArticleCopyright><CopyrightHolderName>Kluwer Academic Publishers</CopyrightHolderName><CopyrightYear>2001</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>11103</JournalID><VolumeIDStart>46</VolumeIDStart><VolumeIDEnd>46</VolumeIDEnd><IssueIDStart>6</IssueIDStart><IssueIDEnd>6</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Sang</GivenName><GivenName>Jik</GivenName><FamilyName>Lee</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Mi-Chung</GivenName><FamilyName>Suh</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>Shinje</GivenName><FamilyName>Kim</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Jin-Kyung</GivenName><FamilyName>Kwon</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Minwoo</GivenName><FamilyName>Kim</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff4"><AuthorName DisplayOrder="Western"><GivenName>Kyung-Hee</GivenName><FamilyName>Paek</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>Doil</GivenName><FamilyName>Choi</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Byung-Dong</GivenName><FamilyName>Kim</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgDivision>School of Plant Science</OrgDivision><OrgName>College of Agriculture and Life Sciences</OrgName><OrgAddress><Country>Korea</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>Plant Cell Biotechnology Laboratory</OrgDivision><OrgName>Korea Research Institute of Bioscience and Biotechnology</OrgName><OrgAddress><City>Taejon</City><Postcode>305-600</Postcode><Country>fKorea</Country></OrgAddress></Affiliation><Affiliation ID="Aff3"><OrgDivision>Center for Plant Molecular Genetics and Breeding Research</OrgDivision><OrgName>Seoul National University</OrgName><OrgAddress><Street>103 Seodoon-dong</Street><City>Suwon</City><Postcode>441-744</Postcode><Country>fKorea</Country></OrgAddress></Affiliation><Affiliation ID="Aff4"><OrgDivision>Plant Molecular Biology and Genetics Laboratory, Graduate School of Biotechnology</OrgDivision><OrgName>Korea University</OrgName><OrgAddress><City>Seoul</City><Postcode>136-701</Postcode><Country>Korea</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>By means of differential display, a pool of salicylic acid (SA)-induced mRNAs were identified and subsequently their cDNAs were isolated from a cDNA library prepared from SA-induced leaf tissues of hot pepper. One of these cDNA clones, designated <Emphasis Type="Italic">CaSIG4</Emphasis>, was 1900 bp and contained an open reading frame encoding 523 amino acids with a calculated molecular mass of 56.3 kDa. The predicted amino acid sequence of <Emphasis Type="Italic">CaSIG4</Emphasis> showed high sequence similarity to the AMP-binding protein family of both prokaryotic and eukaryotic acyl-CoA synthetases. <Emphasis Type="Italic">CaSIG4</Emphasis> transcripts accumulated rapidly after SA treatment and in response to both incompatible and compatible interactions with <Emphasis Type="Italic">Xanthomonas campestris</Emphasis> pv. <Emphasis Type="Italic">vesicatoria</Emphasis> race 1. To investigate the <Emphasis Type="Italic">cis</Emphasis>-acting elements mediating <Emphasis Type="Italic">CaSIG4</Emphasis> expression, the <Emphasis Type="Italic">CaSIG4</Emphasis> 5′-flanking region was isolated by inverse PCR. Database searches indicated that a potential <Emphasis Type="Italic">cis</Emphasis>-regulatory element is almost identical to the consensus core sequences ACC(A/T)ACC(A/C) which are conserved among promoters of other phenylpropanoid biosynthetic genes. The subcellular localization of the CaSIG4 protein was studied by using a soluble modified GFP gene fusion delivered into epidermal cells of onion by biolistic bombardment. The CaSIG4-smGFP fusion protein was localized to the plasma membrane. Taken together, CaSIG4 encoding a putative acyl-CoA synthetase could function as a plasma membrane-bound protein with a role in signaling in plant defense.</Para></Abstract><KeywordGroup Language="En"><Keyword>acyl-CoA synthetase</Keyword><Keyword>AMP-binding protein</Keyword><Keyword><Emphasis Type="Italic">Capsicum annuum</Emphasis> L.</Keyword><Keyword>mRNA differential display</Keyword><Keyword>salicylic acid</Keyword><Keyword>subcellular localization</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Molecular cloning of a novel pathogen-inducible cDNA encoding a putative acyl-CoA synthetase from Capsicum annuum L.</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Molecular cloning of a novel pathogen-inducible cDNA encoding a putative acyl-CoA synthetase from Capsicum annuum L.</title></titleInfo><name type="personal"><namePart type="given">Sang</namePart><namePart type="given">Jik</namePart><namePart type="family">Lee</namePart><affiliation>School of Plant Science, College of Agriculture and Life Sciences, Korea</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Mi-Chung</namePart><namePart type="family">Suh</namePart><affiliation>Plant Cell Biotechnology Laboratory, Korea Research Institute of Bioscience and Biotechnology, 305-600, Taejon, fKorea</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Shinje</namePart><namePart type="family">Kim</namePart><affiliation>Center for Plant Molecular Genetics and Breeding Research, Seoul National University, 103 Seodoon-dong, 441-744, Suwon, fKorea</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jin-Kyung</namePart><namePart type="family">Kwon</namePart><affiliation>School of Plant Science, College of Agriculture and Life Sciences, Korea</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Minwoo</namePart><namePart type="family">Kim</namePart><affiliation>School of Plant Science, College of Agriculture and Life Sciences, Korea</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Kyung-Hee</namePart><namePart type="family">Paek</namePart><affiliation>Plant Molecular Biology and Genetics Laboratory, Graduate School of Biotechnology, Korea University, 136-701, Seoul, Korea</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Doil</namePart><namePart type="family">Choi</namePart><affiliation>Center for Plant Molecular Genetics and Breeding Research, Seoul National University, 103 Seodoon-dong, 441-744, Suwon, fKorea</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Byung-Dong</namePart><namePart type="family">Kim</namePart><affiliation>School of Plant Science, College of Agriculture and Life Sciences, Korea</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Kluwer Academic Publishers</publisher><place><placeTerm type="text">Dordrecht</placeTerm></place><dateIssued encoding="w3cdtf">2001-08-01</dateIssued><copyrightDate encoding="w3cdtf">2001</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: By means of differential display, a pool of salicylic acid (SA)-induced mRNAs were identified and subsequently their cDNAs were isolated from a cDNA library prepared from SA-induced leaf tissues of hot pepper. One of these cDNA clones, designated CaSIG4, was 1900 bp and contained an open reading frame encoding 523 amino acids with a calculated molecular mass of 56.3 kDa. The predicted amino acid sequence of CaSIG4 showed high sequence similarity to the AMP-binding protein family of both prokaryotic and eukaryotic acyl-CoA synthetases. CaSIG4 transcripts accumulated rapidly after SA treatment and in response to both incompatible and compatible interactions with Xanthomonas campestris pv. vesicatoria race 1. To investigate the cis-acting elements mediating CaSIG4 expression, the CaSIG4 5′-flanking region was isolated by inverse PCR. Database searches indicated that a potential cis-regulatory element is almost identical to the consensus core sequences ACC(A/T)ACC(A/C) which are conserved among promoters of other phenylpropanoid biosynthetic genes. The subcellular localization of the CaSIG4 protein was studied by using a soluble modified GFP gene fusion delivered into epidermal cells of onion by biolistic bombardment. The CaSIG4-smGFP fusion protein was localized to the plasma membrane. Taken together, CaSIG4 encoding a putative acyl-CoA synthetase could function as a plasma membrane-bound protein with a role in signaling in plant defense.</abstract><subject lang="en"><topic>acyl-CoA synthetase</topic><topic>AMP-binding protein</topic><topic>Capsicum annuum L.</topic><topic>mRNA differential display</topic><topic>salicylic acid</topic><topic>subcellular localization</topic></subject><relatedItem type="host"><titleInfo><title>Plant Molecular Biology</title><subTitle>An International Journal on Molecular Biology, Molecular Genetics and Biochemistry</subTitle></titleInfo><titleInfo type="abbreviated"><title>Plant Mol Biol</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">2001-08-01</dateIssued><copyrightDate encoding="w3cdtf">2001</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Biochemistry, general</topic><topic>Plant Sciences</topic><topic>Plant Pathology</topic></subject><identifier type="ISSN">0167-4412</identifier><identifier type="eISSN">1573-5028</identifier><identifier type="JournalID">11103</identifier><identifier type="IssueArticleCount">13</identifier><identifier type="VolumeIssueCount">6</identifier><part><date>2001</date><detail type="volume"><number>46</number><caption>vol.</caption></detail><detail type="issue"><number>6</number><caption>no.</caption></detail><extent unit="pages"><start>661</start><end>671</end></extent></part><recordInfo><recordOrigin>Kluwer Academic Publishers, 2001</recordOrigin></recordInfo></relatedItem><identifier type="istex">C8BBDFFE8469105F6A9536EDC71706BB06A78587</identifier><identifier type="ark">ark:/67375/VQC-82XR3V3D-V</identifier><identifier type="DOI">10.1023/A:1011677028605</identifier><identifier type="ArticleID">354101</identifier><identifier type="ArticleID">Art3</identifier><accessCondition type="use and reproduction" contentType="copyright">Kluwer Academic Publishers, 2001</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Kluwer Academic Publishers, 2001</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-82XR3V3D-V/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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