MersV1, Ncbi, Merge, bibRecord, 000029

Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein.

Identifieur interne : 000029 ( Ncbi/Merge ); précédent : 000028; suivant : 000030

Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein.

Auteurs : P. Jekow [Allemagne] ; J. Behlke ; W. Tichelaar ; R. Lurz ; M. Regalla ; W. Hinrichs ; P. Tavares

Source :

European journal of biochemistry [ 0014-2956 ] ; 1999.

RBID : pubmed:10491118

Descripteurs français

English descriptors

KwdEn :
- Bacillus Phages (chemistry), Bacillus Phages (genetics), Cations, Divalent, Centrifugation, Density Gradient, Cross-Linking Reagents, Drug Stability, Glutaral, Microscopy, Electron, Molecular Weight, Osmolar Concentration, Protein Conformation, Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (isolation & purification), Solutions, Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (isolation & purification).
MESH :
- chemical , chemistry : Recombinant Proteins, Viral Proteins.
- chemical , genetics : Recombinant Proteins, Viral Proteins.
- chemical , isolation & purification : Recombinant Proteins, Viral Proteins.
- chemical : Cations, Divalent, Cross-Linking Reagents, Glutaral, Solutions.
- chemistry : Bacillus Phages.
- genetics : Bacillus Phages.
- Centrifugation, Density Gradient, Drug Stability, Microscopy, Electron, Molecular Weight, Osmolar Concentration, Protein Conformation.

Abstract

Bacteriophage SPP1 portal protein is a large cyclical homo-oligomer composed of 13 subunits. The solution structure and assembly behavior of this protein with high-point rotational symmetry was characterized. The purified protein was present as a monodisperse population of 13-mers, named gp6H, at univalent salt concentrations in the hundred millimolar range (>/= 250 mM NaCl) or in the presence of bivalent cations in the millimolar range (>/= 5 mM MgCl2). Gp6H had a slightly higher sedimentation coefficient, a smaller shape-dependent frictional ratio, and a higher rate of intersubunit cross-linking in the presence of magnesium than in its absence. In the absence of bivalent cations and at univalent salt concentrations below 250 mM, the 13-mer molecules dissociated partially into stable monomers, named gp6L. The monomer had a somewhat different shape from the subunit present in the 13-mer, but maintained a defined tertiary structure. The association-dissociation equilibrium was mainly between the monomer and the 13-mer with a minor population of intermediate oligomers. Their interconversion was strongly influenced by the ionic environment. Under physiological conditions, the concentration of Mg2+ found in the Bacillus subtilis cytoplasm (10-50 mM) probably promotes complete association of gp6 into 13-mer rings with a compact conformation.

DOI: 10.1046/j.1432-1327.1999.00601.x
PubMed: 10491118

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 002620
to stream PubMed, to step Curation: 002620
to stream PubMed, to step Checkpoint: 002497

Links to Exploration step

pubmed:10491118

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein.</title>
<author><name sortKey="Jekow, P" sort="Jekow, P" uniqKey="Jekow P" first="P" last="Jekow">P. Jekow</name>
<affiliation wicri:level="3"><nlm:affiliation>Max Planck Institut für Molekulare Genetik, Berlin, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Max Planck Institut für Molekulare Genetik, Berlin</wicri:regionArea>
<placeName><region type="land" nuts="3">Berlin</region>
<settlement type="city">Berlin</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Behlke, J" sort="Behlke, J" uniqKey="Behlke J" first="J" last="Behlke">J. Behlke</name>
</author>
<author><name sortKey="Tichelaar, W" sort="Tichelaar, W" uniqKey="Tichelaar W" first="W" last="Tichelaar">W. Tichelaar</name>
</author>
<author><name sortKey="Lurz, R" sort="Lurz, R" uniqKey="Lurz R" first="R" last="Lurz">R. Lurz</name>
</author>
<author><name sortKey="Regalla, M" sort="Regalla, M" uniqKey="Regalla M" first="M" last="Regalla">M. Regalla</name>
</author>
<author><name sortKey="Hinrichs, W" sort="Hinrichs, W" uniqKey="Hinrichs W" first="W" last="Hinrichs">W. Hinrichs</name>
</author>
<author><name sortKey="Tavares, P" sort="Tavares, P" uniqKey="Tavares P" first="P" last="Tavares">P. Tavares</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="1999">1999</date>
<idno type="RBID">pubmed:10491118</idno>
<idno type="pmid">10491118</idno>
<idno type="doi">10.1046/j.1432-1327.1999.00601.x</idno>
<idno type="wicri:Area/PubMed/Corpus">002620</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002620</idno>
<idno type="wicri:Area/PubMed/Curation">002620</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002620</idno>
<idno type="wicri:Area/PubMed/Checkpoint">002497</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002497</idno>
<idno type="wicri:Area/Ncbi/Merge">000029</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein.</title>
<author><name sortKey="Jekow, P" sort="Jekow, P" uniqKey="Jekow P" first="P" last="Jekow">P. Jekow</name>
<affiliation wicri:level="3"><nlm:affiliation>Max Planck Institut für Molekulare Genetik, Berlin, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Max Planck Institut für Molekulare Genetik, Berlin</wicri:regionArea>
<placeName><region type="land" nuts="3">Berlin</region>
<settlement type="city">Berlin</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Behlke, J" sort="Behlke, J" uniqKey="Behlke J" first="J" last="Behlke">J. Behlke</name>
</author>
<author><name sortKey="Tichelaar, W" sort="Tichelaar, W" uniqKey="Tichelaar W" first="W" last="Tichelaar">W. Tichelaar</name>
</author>
<author><name sortKey="Lurz, R" sort="Lurz, R" uniqKey="Lurz R" first="R" last="Lurz">R. Lurz</name>
</author>
<author><name sortKey="Regalla, M" sort="Regalla, M" uniqKey="Regalla M" first="M" last="Regalla">M. Regalla</name>
</author>
<author><name sortKey="Hinrichs, W" sort="Hinrichs, W" uniqKey="Hinrichs W" first="W" last="Hinrichs">W. Hinrichs</name>
</author>
<author><name sortKey="Tavares, P" sort="Tavares, P" uniqKey="Tavares P" first="P" last="Tavares">P. Tavares</name>
</author>
</analytic>
<series><title level="j">European journal of biochemistry</title>
<idno type="ISSN">0014-2956</idno>
<imprint><date when="1999" type="published">1999</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacillus Phages (chemistry)</term>
<term>Bacillus Phages (genetics)</term>
<term>Cations, Divalent</term>
<term>Centrifugation, Density Gradient</term>
<term>Cross-Linking Reagents</term>
<term>Drug Stability</term>
<term>Glutaral</term>
<term>Microscopy, Electron</term>
<term>Molecular Weight</term>
<term>Osmolar Concentration</term>
<term>Protein Conformation</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (isolation & purification)</term>
<term>Solutions</term>
<term>Viral Proteins (chemistry)</term>
<term>Viral Proteins (genetics)</term>
<term>Viral Proteins (isolation & purification)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cations divalents</term>
<term>Centrifugation en gradient de densité</term>
<term>Concentration osmolaire</term>
<term>Conformation des protéines</term>
<term>Glutaraldéhyde</term>
<term>Masse moléculaire</term>
<term>Microscopie électronique</term>
<term>Phages de Bacillus ()</term>
<term>Phages de Bacillus (génétique)</term>
<term>Protéines recombinantes ()</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (isolement et purification)</term>
<term>Protéines virales ()</term>
<term>Protéines virales (génétique)</term>
<term>Protéines virales (isolement et purification)</term>
<term>Réactifs réticulants</term>
<term>Solutions</term>
<term>Stabilité de médicament</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Recombinant Proteins</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Recombinant Proteins</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Recombinant Proteins</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cations, Divalent</term>
<term>Cross-Linking Reagents</term>
<term>Glutaral</term>
<term>Solutions</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Bacillus Phages</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Bacillus Phages</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Phages de Bacillus</term>
<term>Protéines recombinantes</term>
<term>Protéines virales</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines recombinantes</term>
<term>Protéines virales</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Centrifugation, Density Gradient</term>
<term>Drug Stability</term>
<term>Microscopy, Electron</term>
<term>Molecular Weight</term>
<term>Osmolar Concentration</term>
<term>Protein Conformation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cations divalents</term>
<term>Centrifugation en gradient de densité</term>
<term>Concentration osmolaire</term>
<term>Conformation des protéines</term>
<term>Glutaraldéhyde</term>
<term>Masse moléculaire</term>
<term>Microscopie électronique</term>
<term>Phages de Bacillus</term>
<term>Protéines recombinantes</term>
<term>Protéines virales</term>
<term>Réactifs réticulants</term>
<term>Solutions</term>
<term>Stabilité de médicament</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Bacteriophage SPP1 portal protein is a large cyclical homo-oligomer composed of 13 subunits. The solution structure and assembly behavior of this protein with high-point rotational symmetry was characterized. The purified protein was present as a monodisperse population of 13-mers, named gp6H, at univalent salt concentrations in the hundred millimolar range (>/= 250 mM NaCl) or in the presence of bivalent cations in the millimolar range (>/= 5 mM MgCl2). Gp6H had a slightly higher sedimentation coefficient, a smaller shape-dependent frictional ratio, and a higher rate of intersubunit cross-linking in the presence of magnesium than in its absence. In the absence of bivalent cations and at univalent salt concentrations below 250 mM, the 13-mer molecules dissociated partially into stable monomers, named gp6L. The monomer had a somewhat different shape from the subunit present in the 13-mer, but maintained a defined tertiary structure. The association-dissociation equilibrium was mainly between the monomer and the 13-mer with a minor population of intermediate oligomers. Their interconversion was strongly influenced by the ionic environment. Under physiological conditions, the concentration of Mg2+ found in the Bacillus subtilis cytoplasm (10-50 mM) probably promotes complete association of gp6 into 13-mer rings with a compact conformation.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10491118</PMID>
<DateCompleted><Year>1999</Year>
<Month>10</Month>
<Day>14</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>06</Month>
<Day>20</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-2956</ISSN>
<JournalIssue CitedMedium="Print"><Volume>264</Volume>
<Issue>3</Issue>
<PubDate><Year>1999</Year>
<Month>Sep</Month>
</PubDate>
</JournalIssue>
<Title>European journal of biochemistry</Title>
<ISOAbbreviation>Eur. J. Biochem.</ISOAbbreviation>
</Journal>
<ArticleTitle>Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein.</ArticleTitle>
<Pagination><MedlinePgn>724-35</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Bacteriophage SPP1 portal protein is a large cyclical homo-oligomer composed of 13 subunits. The solution structure and assembly behavior of this protein with high-point rotational symmetry was characterized. The purified protein was present as a monodisperse population of 13-mers, named gp6H, at univalent salt concentrations in the hundred millimolar range (>/= 250 mM NaCl) or in the presence of bivalent cations in the millimolar range (>/= 5 mM MgCl2). Gp6H had a slightly higher sedimentation coefficient, a smaller shape-dependent frictional ratio, and a higher rate of intersubunit cross-linking in the presence of magnesium than in its absence. In the absence of bivalent cations and at univalent salt concentrations below 250 mM, the 13-mer molecules dissociated partially into stable monomers, named gp6L. The monomer had a somewhat different shape from the subunit present in the 13-mer, but maintained a defined tertiary structure. The association-dissociation equilibrium was mainly between the monomer and the 13-mer with a minor population of intermediate oligomers. Their interconversion was strongly influenced by the ionic environment. Under physiological conditions, the concentration of Mg2+ found in the Bacillus subtilis cytoplasm (10-50 mM) probably promotes complete association of gp6 into 13-mer rings with a compact conformation.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jekow</LastName>
<ForeName>P</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Max Planck Institut für Molekulare Genetik, Berlin, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Behlke</LastName>
<ForeName>J</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Tichelaar</LastName>
<ForeName>W</ForeName>
<Initials>W</Initials>
</Author>
<Author ValidYN="Y"><LastName>Lurz</LastName>
<ForeName>R</ForeName>
<Initials>R</Initials>
</Author>
<Author ValidYN="Y"><LastName>Regalla</LastName>
<ForeName>M</ForeName>
<Initials>M</Initials>
</Author>
<Author ValidYN="Y"><LastName>Hinrichs</LastName>
<ForeName>W</ForeName>
<Initials>W</Initials>
</Author>
<Author ValidYN="Y"><LastName>Tavares</LastName>
<ForeName>P</ForeName>
<Initials>P</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Eur J Biochem</MedlineTA>
<NlmUniqueID>0107600</NlmUniqueID>
<ISSNLinking>0014-2956</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D002413">Cations, Divalent</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D003432">Cross-Linking Reagents</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D012996">Solutions</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C115880">portal protein, Bacteriophage SPP1</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>T3C89M417N</RegistryNumber>
<NameOfSubstance UI="D005976">Glutaral</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D017103" MajorTopicYN="N">Bacillus Phages</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002413" MajorTopicYN="N">Cations, Divalent</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002499" MajorTopicYN="N">Centrifugation, Density Gradient</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003432" MajorTopicYN="N">Cross-Linking Reagents</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004355" MajorTopicYN="N">Drug Stability</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005976" MajorTopicYN="N">Glutaral</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008854" MajorTopicYN="N">Microscopy, Electron</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009994" MajorTopicYN="N">Osmolar Concentration</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012996" MajorTopicYN="N">Solutions</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year>
<Month>9</Month>
<Day>22</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>1999</Year>
<Month>9</Month>
<Day>22</Day>
<Hour>0</Hour>
<Minute>1</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>1999</Year>
<Month>9</Month>
<Day>22</Day>
<Hour>0</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">10491118</ArticleId>
<ArticleId IdType="pii">ejb601</ArticleId>
<ArticleId IdType="doi">10.1046/j.1432-1327.1999.00601.x</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Allemagne</li>
</country>
<region><li>Berlin</li>
</region>
<settlement><li>Berlin</li>
</settlement>
</list>
<tree><noCountry><name sortKey="Behlke, J" sort="Behlke, J" uniqKey="Behlke J" first="J" last="Behlke">J. Behlke</name>
<name sortKey="Hinrichs, W" sort="Hinrichs, W" uniqKey="Hinrichs W" first="W" last="Hinrichs">W. Hinrichs</name>
<name sortKey="Lurz, R" sort="Lurz, R" uniqKey="Lurz R" first="R" last="Lurz">R. Lurz</name>
<name sortKey="Regalla, M" sort="Regalla, M" uniqKey="Regalla M" first="M" last="Regalla">M. Regalla</name>
<name sortKey="Tavares, P" sort="Tavares, P" uniqKey="Tavares P" first="P" last="Tavares">P. Tavares</name>
<name sortKey="Tichelaar, W" sort="Tichelaar, W" uniqKey="Tichelaar W" first="W" last="Tichelaar">W. Tichelaar</name>
</noCountry>
<country name="Allemagne"><region name="Berlin"><name sortKey="Jekow, P" sort="Jekow, P" uniqKey="Jekow P" first="P" last="Jekow">P. Jekow</name>
</region>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Ncbi/Merge

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000029 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd -nk 000029 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    MersV1
   |flux=    Ncbi
   |étape=   Merge
   |type=    RBID
   |clé=     pubmed:10491118
   |texte=   Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/RBID.i   -Sk "pubmed:10491118" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd   \
       | NlmPubMed2Wicri -a MersV1

This area was generated with Dilib version V0.6.33.
Data generation: Mon Apr 20 23:26:43 2020. Site generation: Sat Mar 27 09:06:09 2021

	Serveur d'exploration MERS
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration MERS

Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein.

Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki