Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ribonucleocapsid assembly in vivo
Identifieur interne : 000C15 ( Istex/Corpus ); précédent : 000C14; suivant : 000C16Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ribonucleocapsid assembly in vivo
Auteurs : D.-J. Hwang ; N. E. Tumer ; T. M. A. WilsonSource :
- Archives of Virology [ 0304-8608 ] ; 1998-11-01.
Abstract
Summary: Several prokaryotic chaperone proteins were shown to promote the correct folding and in vivo assembly of tobacco mosaic virus coat protein (TMV CP) using a chimaeric RNA packaging system in control or chaperone-deficient mutant strains of Escherichia coli. Mutations in groEL or dnaK reduced the amount of both total and soluble TMV CP, and the yield of assembled TMV-like particles, several-fold. Thus both GroEL and DnaK have significant direct or indirect effects on the overall expression, stability, folding and assembly of TMV CP in vivo. In contrast, while cells carrying a mutation in grpE expressed TMV CP to a higher overall level than control E. coli, the amounts of both soluble CP and assembled TMV-like particles were below control levels, suggesting a negative effect of GrpE on overall CP accumulation, but positive role(s) in CP folding and assembly. Curiously, cells with mutations in groES and, to a lesser extent, dnaJ expressed total, soluble and assembled forms of TMV CP significantly above control values, suggesting some form of negative control by these chaperone proteins. To avoid pleiotropic effects or artefacts in chaperone- null mutants, selected chaperone proteins were also over-expressed in control E. coli cells. Overproduction of GroEL or GroES alone had little effect. However, co-overexpression of GroEL and GroES resulted in a two-fold increase in soluble TMV CP and a four-fold rise in assembled TMV-like (pseudovirus) particles in vivo. Moreover, TMV CP was shown to interact directly with GroEL in vivo. Together, these results suggest that GrpE and the GroEL/GroES chaper- one complex promote the correct folding and assembly of TMV CP into ribonucleocapsids in vivo.
Url:
DOI: 10.1007/s007050050452
Links to Exploration step
ISTEX:63770C6251FEABE6B4C924C1C7248BDA3F514863Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ribonucleocapsid assembly in vivo</title><author><name sortKey="Hwang, D J" sort="Hwang, D J" uniqKey="Hwang D" first="D.-J." last="Hwang">D.-J. Hwang</name><affiliation><mods:affiliation>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A., USA</mods:affiliation></affiliation></author><author><name sortKey="Tumer, N E" sort="Tumer, N E" uniqKey="Tumer N" first="N. E." last="Tumer">N. E. Tumer</name><affiliation><mods:affiliation>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A., USA</mods:affiliation></affiliation></author><author><name sortKey="Wilson, T M A" sort="Wilson, T M A" uniqKey="Wilson T" first="T. M. A." last="Wilson">T. M. A. Wilson</name><affiliation><mods:affiliation>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A., USA</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:63770C6251FEABE6B4C924C1C7248BDA3F514863</idno><date when="1998" year="1998">1998</date><idno type="doi">10.1007/s007050050452</idno><idno type="url">https://api.istex.fr/ark:/67375/VQC-9CJPFMHT-Z/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000C15</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000C15</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ribonucleocapsid assembly in vivo</title><author><name sortKey="Hwang, D J" sort="Hwang, D J" uniqKey="Hwang D" first="D.-J." last="Hwang">D.-J. Hwang</name><affiliation><mods:affiliation>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A., USA</mods:affiliation></affiliation></author><author><name sortKey="Tumer, N E" sort="Tumer, N E" uniqKey="Tumer N" first="N. E." last="Tumer">N. E. Tumer</name><affiliation><mods:affiliation>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A., USA</mods:affiliation></affiliation></author><author><name sortKey="Wilson, T M A" sort="Wilson, T M A" uniqKey="Wilson T" first="T. M. A." last="Wilson">T. M. A. Wilson</name><affiliation><mods:affiliation>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A., USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Archives of Virology</title><title level="j" type="abbrev">Arch. Virol.</title><idno type="ISSN">0304-8608</idno><idno type="eISSN">1432-8798</idno><imprint><publisher>Springer-Verlag</publisher><pubPlace>Vienna</pubPlace><date type="published" when="1998-11-01">1998-11-01</date><biblScope unit="volume">143</biblScope><biblScope unit="issue">11</biblScope><biblScope unit="page" from="2203">2203</biblScope><biblScope unit="page" to="2214">2214</biblScope></imprint><idno type="ISSN">0304-8608</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0304-8608</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Summary: Several prokaryotic chaperone proteins were shown to promote the correct folding and in vivo assembly of tobacco mosaic virus coat protein (TMV CP) using a chimaeric RNA packaging system in control or chaperone-deficient mutant strains of Escherichia coli. Mutations in groEL or dnaK reduced the amount of both total and soluble TMV CP, and the yield of assembled TMV-like particles, several-fold. Thus both GroEL and DnaK have significant direct or indirect effects on the overall expression, stability, folding and assembly of TMV CP in vivo. In contrast, while cells carrying a mutation in grpE expressed TMV CP to a higher overall level than control E. coli, the amounts of both soluble CP and assembled TMV-like particles were below control levels, suggesting a negative effect of GrpE on overall CP accumulation, but positive role(s) in CP folding and assembly. Curiously, cells with mutations in groES and, to a lesser extent, dnaJ expressed total, soluble and assembled forms of TMV CP significantly above control values, suggesting some form of negative control by these chaperone proteins. To avoid pleiotropic effects or artefacts in chaperone- null mutants, selected chaperone proteins were also over-expressed in control E. coli cells. Overproduction of GroEL or GroES alone had little effect. However, co-overexpression of GroEL and GroES resulted in a two-fold increase in soluble TMV CP and a four-fold rise in assembled TMV-like (pseudovirus) particles in vivo. Moreover, TMV CP was shown to interact directly with GroEL in vivo. Together, these results suggest that GrpE and the GroEL/GroES chaper- one complex promote the correct folding and assembly of TMV CP into ribonucleocapsids in vivo.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>D.-J. Hwang</name><affiliations><json:string>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A., USA</json:string></affiliations></json:item><json:item><name>N. E. Tumer</name><affiliations><json:string>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A., USA</json:string></affiliations></json:item><json:item><name>T. M. A. Wilson</name><affiliations><json:string>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A., USA</json:string></affiliations></json:item></author><articleId><json:string>81432203</json:string><json:string>Art9</json:string></articleId><arkIstex>ark:/67375/VQC-9CJPFMHT-Z</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Summary: Several prokaryotic chaperone proteins were shown to promote the correct folding and in vivo assembly of tobacco mosaic virus coat protein (TMV CP) using a chimaeric RNA packaging system in control or chaperone-deficient mutant strains of Escherichia coli. Mutations in groEL or dnaK reduced the amount of both total and soluble TMV CP, and the yield of assembled TMV-like particles, several-fold. Thus both GroEL and DnaK have significant direct or indirect effects on the overall expression, stability, folding and assembly of TMV CP in vivo. In contrast, while cells carrying a mutation in grpE expressed TMV CP to a higher overall level than control E. coli, the amounts of both soluble CP and assembled TMV-like particles were below control levels, suggesting a negative effect of GrpE on overall CP accumulation, but positive role(s) in CP folding and assembly. Curiously, cells with mutations in groES and, to a lesser extent, dnaJ expressed total, soluble and assembled forms of TMV CP significantly above control values, suggesting some form of negative control by these chaperone proteins. To avoid pleiotropic effects or artefacts in chaperone- null mutants, selected chaperone proteins were also over-expressed in control E. coli cells. Overproduction of GroEL or GroES alone had little effect. However, co-overexpression of GroEL and GroES resulted in a two-fold increase in soluble TMV CP and a four-fold rise in assembled TMV-like (pseudovirus) particles in vivo. Moreover, TMV CP was shown to interact directly with GroEL in vivo. 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Virol.</title><idno type="pISSN">0304-8608</idno><idno type="eISSN">1432-8798</idno><idno type="journal-ID">true</idno><idno type="issue-article-count">16</idno><idno type="volume-issue-count">12</idno><imprint><publisher>Springer-Verlag</publisher><pubPlace>Vienna</pubPlace><date type="published" when="1998-11-01"></date><biblScope unit="volume">143</biblScope><biblScope unit="issue">11</biblScope><biblScope unit="page" from="2203">2203</biblScope><biblScope unit="page" to="2214">2214</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1998</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Summary: Several prokaryotic chaperone proteins were shown to promote the correct folding and in vivo assembly of tobacco mosaic virus coat protein (TMV CP) using a chimaeric RNA packaging system in control or chaperone-deficient mutant strains of Escherichia coli. Mutations in groEL or dnaK reduced the amount of both total and soluble TMV CP, and the yield of assembled TMV-like particles, several-fold. Thus both GroEL and DnaK have significant direct or indirect effects on the overall expression, stability, folding and assembly of TMV CP in vivo. In contrast, while cells carrying a mutation in grpE expressed TMV CP to a higher overall level than control E. coli, the amounts of both soluble CP and assembled TMV-like particles were below control levels, suggesting a negative effect of GrpE on overall CP accumulation, but positive role(s) in CP folding and assembly. Curiously, cells with mutations in groES and, to a lesser extent, dnaJ expressed total, soluble and assembled forms of TMV CP significantly above control values, suggesting some form of negative control by these chaperone proteins. To avoid pleiotropic effects or artefacts in chaperone- null mutants, selected chaperone proteins were also over-expressed in control E. coli cells. Overproduction of GroEL or GroES alone had little effect. However, co-overexpression of GroEL and GroES resulted in a two-fold increase in soluble TMV CP and a four-fold rise in assembled TMV-like (pseudovirus) particles in vivo. Moreover, TMV CP was shown to interact directly with GroEL in vivo. Together, these results suggest that GrpE and the GroEL/GroES chaper- one complex promote the correct folding and assembly of TMV CP into ribonucleocapsids in vivo.</p></abstract><textClass><keywords scheme="Journal-Subject-Group"><list><label>SCB</label><item><term>Biomedicine</term></item><label>SCB22003</label><item><term>Virology</term></item><label>SCB16003</label><item><term>Medical Microbiology</term></item><label>SCH33096</label><item><term>Infectious Diseases</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998-11-01">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-9CJPFMHT-Z/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus springer-journals not found" wicri:toSee="no header"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//Springer-Verlag//DTD A++ V2.4//EN" URI="http://devel.springer.de/A++/V2.4/DTD/A++V2.4.dtd" name="istex:docType"></istex:docType><istex:document><Publisher><PublisherInfo><PublisherName>Springer-Verlag</PublisherName><PublisherLocation>Vienna</PublisherLocation></PublisherInfo><Journal><JournalInfo JournalProductType="ArchiveJournal" NumberingStyle="Unnumbered"><JournalID>705</JournalID><JournalPrintISSN>0304-8608</JournalPrintISSN><JournalElectronicISSN>1432-8798</JournalElectronicISSN><JournalTitle>Archives of Virology</JournalTitle><JournalAbbreviatedTitle>Arch. Virol.</JournalAbbreviatedTitle><JournalSubjectGroup><JournalSubject Code="SCB" Type="Primary">Biomedicine</JournalSubject><JournalSubject Code="SCB22003" Priority="1" Type="Secondary">Virology</JournalSubject><JournalSubject Code="SCB16003" Priority="2" Type="Secondary">Medical Microbiology</JournalSubject><JournalSubject Code="SCH33096" Priority="3" Type="Secondary">Infectious Diseases</JournalSubject></JournalSubjectGroup></JournalInfo><Volume><VolumeInfo TocLevels="0" VolumeType="Regular"><VolumeIDStart>143</VolumeIDStart><VolumeIDEnd>143</VolumeIDEnd><VolumeIssueCount>12</VolumeIssueCount></VolumeInfo><Issue IssueType="Regular"><IssueInfo TocLevels="0"><IssueIDStart>11</IssueIDStart><IssueIDEnd>11</IssueIDEnd><IssueArticleCount>16</IssueArticleCount><IssueHistory><CoverDate><Year>1998</Year><Month>11</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>1998</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art9"><ArticleInfo ArticleType="OriginalPaper" ContainsESM="No" Language="En" NumberingStyle="Unnumbered" TocLevels="0"><ArticleID>81432203</ArticleID><ArticleDOI>10.1007/s007050050452</ArticleDOI><ArticleSequenceNumber>9</ArticleSequenceNumber><ArticleTitle Language="En">Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ribonucleocapsid assembly in vivo</ArticleTitle><ArticleFirstPage>2203</ArticleFirstPage><ArticleLastPage>2214</ArticleLastPage><ArticleHistory><RegistrationDate><Year>1998</Year><Month>4</Month><Day>8</Day></RegistrationDate><OnlineDate><Year>2014</Year><Month>4</Month><Day>8</Day></OnlineDate></ArticleHistory><ArticleCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>1998</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></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>D.-J.</GivenName><FamilyName>Hwang</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>N.</GivenName><GivenName>E.</GivenName><FamilyName>Tumer</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>T.</GivenName><GivenName>M.</GivenName><GivenName>A.</GivenName><FamilyName>Wilson</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgName>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A.</OrgName><OrgAddress><Country>USA</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Summary</Heading><Para>Several prokaryotic chaperone proteins were shown to promote the correct folding and in vivo assembly of tobacco mosaic virus coat protein (TMV CP) using a chimaeric RNA packaging system in control or chaperone-deficient mutant strains of <Emphasis Type="Italic">Escherichia coli</Emphasis>. Mutations in <Emphasis Type="Italic">groEL</Emphasis> or <Emphasis Type="Italic">dnaK</Emphasis> reduced the amount of both total and soluble TMV CP, and the yield of assembled TMV-like particles, several-fold. Thus both GroEL and DnaK have significant direct or indirect effects on the overall expression, stability, folding and assembly of TMV CP in vivo. In contrast, while cells carrying a mutation in <Emphasis Type="Italic">grpE</Emphasis> expressed TMV CP to a higher overall level than control <Emphasis Type="Italic">E. coli</Emphasis>, the amounts of both soluble CP and assembled TMV-like particles were below control levels, suggesting a negative effect of GrpE on overall CP accumulation, but positive role(s) in CP folding and assembly. Curiously, cells with mutations in <Emphasis Type="Italic">groES</Emphasis> and, to a lesser extent, <Emphasis Type="Italic">dnaJ</Emphasis> expressed total, soluble and assembled forms of TMV CP significantly above control values, suggesting some form of negative control by these chaperone proteins. To avoid pleiotropic effects or artefacts in chaperone- null mutants, selected chaperone proteins were also over-expressed in control <Emphasis Type="Italic">E. coli</Emphasis> cells. Overproduction of GroEL or GroES alone had little effect. However, co-overexpression of GroEL and GroES resulted in a two-fold increase in soluble TMV CP and a four-fold rise in assembled TMV-like (pseudovirus) particles in vivo. Moreover, TMV CP was shown to interact directly with GroEL in vivo. Together, these results suggest that GrpE and the GroEL/GroES chaper- one complex promote the correct folding and assembly of TMV CP into ribonucleocapsids in vivo.</Para></Abstract><ArticleNote Type="Misc"><SimplePara>Received April 14, 1998 Accepted June 19, 1998</SimplePara></ArticleNote></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ribonucleocapsid assembly in vivo</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ribonucleocapsid assembly in vivo</title></titleInfo><name type="personal"><namePart type="given">D.-J.</namePart><namePart type="family">Hwang</namePart><affiliation>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A., USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">N.</namePart><namePart type="given">E.</namePart><namePart type="family">Tumer</namePart><affiliation>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A., USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">T.</namePart><namePart type="given">M.</namePart><namePart type="given">A.</namePart><namePart type="family">Wilson</namePart><affiliation>AgBiotech Center, Cook College, Rutgers University, New Brunswick, New Jersey, U.S.A., USA</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>Springer-Verlag</publisher><place><placeTerm type="text">Vienna</placeTerm></place><dateIssued encoding="w3cdtf">1998-11-01</dateIssued><copyrightDate encoding="w3cdtf">1998</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Summary: Several prokaryotic chaperone proteins were shown to promote the correct folding and in vivo assembly of tobacco mosaic virus coat protein (TMV CP) using a chimaeric RNA packaging system in control or chaperone-deficient mutant strains of Escherichia coli. Mutations in groEL or dnaK reduced the amount of both total and soluble TMV CP, and the yield of assembled TMV-like particles, several-fold. Thus both GroEL and DnaK have significant direct or indirect effects on the overall expression, stability, folding and assembly of TMV CP in vivo. In contrast, while cells carrying a mutation in grpE expressed TMV CP to a higher overall level than control E. coli, the amounts of both soluble CP and assembled TMV-like particles were below control levels, suggesting a negative effect of GrpE on overall CP accumulation, but positive role(s) in CP folding and assembly. Curiously, cells with mutations in groES and, to a lesser extent, dnaJ expressed total, soluble and assembled forms of TMV CP significantly above control values, suggesting some form of negative control by these chaperone proteins. To avoid pleiotropic effects or artefacts in chaperone- null mutants, selected chaperone proteins were also over-expressed in control E. coli cells. Overproduction of GroEL or GroES alone had little effect. However, co-overexpression of GroEL and GroES resulted in a two-fold increase in soluble TMV CP and a four-fold rise in assembled TMV-like (pseudovirus) particles in vivo. Moreover, TMV CP was shown to interact directly with GroEL in vivo. Together, these results suggest that GrpE and the GroEL/GroES chaper- one complex promote the correct folding and assembly of TMV CP into ribonucleocapsids in vivo.</abstract><relatedItem type="host"><titleInfo><title>Archives of Virology</title></titleInfo><titleInfo type="abbreviated"><title>Arch. Virol.</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">1998-11-01</dateIssued><copyrightDate encoding="w3cdtf">1998</copyrightDate></originInfo><subject><genre>Journal-Subject-Group</genre><topic authority="SpringerSubjectCodes" authorityURI="SCB">Biomedicine</topic><topic authority="SpringerSubjectCodes" authorityURI="SCB22003">Virology</topic><topic authority="SpringerSubjectCodes" authorityURI="SCB16003">Medical Microbiology</topic><topic authority="SpringerSubjectCodes" authorityURI="SCH33096">Infectious Diseases</topic></subject><identifier type="ISSN">0304-8608</identifier><identifier type="eISSN">1432-8798</identifier><identifier type="JournalID">705</identifier><identifier type="IssueArticleCount">16</identifier><identifier type="VolumeIssueCount">12</identifier><part><date>1998</date><detail type="volume"><number>143</number><caption>vol.</caption></detail><detail type="issue"><number>11</number><caption>no.</caption></detail><extent unit="pages"><start>2203</start><end>2214</end></extent></part><recordInfo><recordOrigin>Springer-Verlag, 1998</recordOrigin></recordInfo></relatedItem><identifier type="istex">63770C6251FEABE6B4C924C1C7248BDA3F514863</identifier><identifier type="ark">ark:/67375/VQC-9CJPFMHT-Z</identifier><identifier type="DOI">10.1007/s007050050452</identifier><identifier type="ArticleID">81432203</identifier><identifier type="ArticleID">Art9</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer-Verlag, 1998</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>Springer-Verlag, 1998</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-9CJPFMHT-Z/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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