Tripartite regulation of Gln3p by TOR, Ure2p, and phosphatases.
Identifieur interne : 001A27 ( Main/Exploration ); précédent : 001A26; suivant : 001A28Tripartite regulation of Gln3p by TOR, Ure2p, and phosphatases.
Auteurs : P G Bertram [États-Unis] ; J H Choi ; J. Carvalho ; W. Ai ; C. Zeng ; T F Chan ; X F ZhengSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2000.
Descripteurs français
- KwdFr :
- ARN messager (génétique), ARN messager (métabolisme), Facteurs de transcription (métabolisme), Glutathione peroxidase (MeSH), Liaison aux protéines (MeSH), Modèles génétiques (MeSH), Mutation (MeSH), Phosphatidylinositol 3-kinases (MeSH), Phosphoric monoester hydrolases (génétique), Phosphoric monoester hydrolases (métabolisme), Phosphorylation (MeSH), Phosphotransferases (Alcohol Group Acceptor) (composition chimique), Phosphotransferases (Alcohol Group Acceptor) (génétique), Phosphotransferases (Alcohol Group Acceptor) (métabolisme), Prions (MeSH), Protéines de Saccharomyces cerevisiae (MeSH), Protéines de fusion recombinantes (MeSH), Protéines de liaison à l'ADN (métabolisme), Protéines de répression (métabolisme), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Protéines nucléaires (métabolisme), Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Structure tertiaire des protéines (MeSH), Tacrolimus (pharmacologie), Technique d'immunofluorescence (MeSH), Techniques de double hybride (MeSH), Transport des protéines (effets des médicaments et des substances chimiques).
- MESH :
- composition chimique : Phosphotransferases (Alcohol Group Acceptor), Protéines fongiques.
- effets des médicaments et des substances chimiques : Régulation de l'expression des gènes fongiques, Transport des protéines.
- enzymologie : Saccharomyces cerevisiae.
- génétique : ARN messager, Phosphoric monoester hydrolases, Phosphotransferases (Alcohol Group Acceptor), Protéines fongiques, Saccharomyces cerevisiae.
- métabolisme : ARN messager, Facteurs de transcription, Phosphoric monoester hydrolases, Phosphotransferases (Alcohol Group Acceptor), Protéines de liaison à l'ADN, Protéines de répression, Protéines fongiques, Protéines nucléaires, Saccharomyces cerevisiae.
- pharmacologie : Sirolimus, Tacrolimus.
- Glutathione peroxidase, Liaison aux protéines, Modèles génétiques, Mutation, Phosphatidylinositol 3-kinases, Phosphorylation, Prions, Protéines de Saccharomyces cerevisiae, Protéines de fusion recombinantes, Structure tertiaire des protéines, Technique d'immunofluorescence, Techniques de double hybride.
English descriptors
- KwdEn :
- DNA-Binding Proteins (metabolism), Fluorescent Antibody Technique (MeSH), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression Regulation, Fungal (drug effects), Glutathione Peroxidase (MeSH), Models, Genetic (MeSH), Mutation (MeSH), Nuclear Proteins (metabolism), Phosphatidylinositol 3-Kinases (MeSH), Phosphoric Monoester Hydrolases (genetics), Phosphoric Monoester Hydrolases (metabolism), Phosphorylation (MeSH), Phosphotransferases (Alcohol Group Acceptor) (chemistry), Phosphotransferases (Alcohol Group Acceptor) (genetics), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Prions (MeSH), Protein Binding (MeSH), Protein Structure, Tertiary (MeSH), Protein Transport (drug effects), RNA, Messenger (genetics), RNA, Messenger (metabolism), Recombinant Fusion Proteins (MeSH), Repressor Proteins (metabolism), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (MeSH), Sirolimus (pharmacology), Tacrolimus (pharmacology), Transcription Factors (metabolism), Two-Hybrid System Techniques (MeSH).
- MESH :
- chemical , chemistry : Fungal Proteins, Phosphotransferases (Alcohol Group Acceptor).
- chemical , genetics : Fungal Proteins, Phosphoric Monoester Hydrolases, Phosphotransferases (Alcohol Group Acceptor), RNA, Messenger.
- chemical , metabolism : DNA-Binding Proteins, Fungal Proteins, Nuclear Proteins, Phosphoric Monoester Hydrolases, Phosphotransferases (Alcohol Group Acceptor), RNA, Messenger, Repressor Proteins, Transcription Factors.
- drug effects : Gene Expression Regulation, Fungal, Protein Transport.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- chemical , pharmacology : Sirolimus, Tacrolimus.
- Fluorescent Antibody Technique, Glutathione Peroxidase, Models, Genetic, Mutation, Phosphatidylinositol 3-Kinases, Phosphorylation, Prions, Protein Binding, Protein Structure, Tertiary, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins, Two-Hybrid System Techniques.
Abstract
Gln3p is a GATA-type transcription factor responsive to different nitrogen nutrients and starvation in yeast Saccharomyces cerevisiae. Recent evidence has linked TOR signaling to Gln3p. Rapamycin causes dephosphorylation and nuclear translocation of Gln3p, thereby activating nitrogen catabolite repressible-sensitive genes. However, a detailed mechanistic understanding of this process is lacking. In this study, we show that Tor1p physically interacts with Gln3p. An intact TOR kinase domain is essential for the phosphorylation of Gln3p, inhibition of Gln3p nuclear entry and repression of Gln3p-dependent transcription. In contrast, at least two distinct protein phosphatases, Pph3p and the Tap42p-dependent phosphatases, are involved in the activation of Gln3p. The yeast pro-prion protein Ure2p binds to both hyper- and hypo-phosphorylated Gln3p. In contrast to the free Gln3p, the Ure2p-bound Gln3p is signifcantly resistant to dephosphorylation. Taken together, these results reveal a tripartite regulatory mechanism by which the phosphorylation of Gln3p is regulated.
DOI: 10.1074/jbc.M004235200
PubMed: 10940301
Affiliations:
- États-Unis
- Missouri (État)
- Saint-Louis (Missouri)
- École de médecine (Université Washington de Saint-Louis)
Links toward previous steps (curation, corpus...)
Le document en format XML
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3-Kinases (MeSH)</term><term>Phosphoric Monoester Hydrolases (genetics)</term><term>Phosphoric Monoester Hydrolases (metabolism)</term><term>Phosphorylation (MeSH)</term><term>Phosphotransferases (Alcohol Group Acceptor) (chemistry)</term><term>Phosphotransferases (Alcohol Group Acceptor) (genetics)</term><term>Phosphotransferases (Alcohol Group Acceptor) (metabolism)</term><term>Prions (MeSH)</term><term>Protein Binding (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Protein Transport (drug effects)</term><term>RNA, Messenger (genetics)</term><term>RNA, Messenger (metabolism)</term><term>Recombinant Fusion Proteins (MeSH)</term><term>Repressor Proteins (metabolism)</term><term>Saccharomyces cerevisiae (enzymology)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (MeSH)</term><term>Sirolimus (pharmacology)</term><term>Tacrolimus (pharmacology)</term><term>Transcription 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(métabolisme)</term><term>Protéines de répression (métabolisme)</term><term>Protéines fongiques (composition chimique)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Protéines nucléaires (métabolisme)</term><term>Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (enzymologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sirolimus (pharmacologie)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Tacrolimus (pharmacologie)</term><term>Technique d'immunofluorescence (MeSH)</term><term>Techniques de double hybride (MeSH)</term><term>Transport des protéines (effets des médicaments et des substances chimiques)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term><term>Phosphotransferases (Alcohol Group 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transcription</term><term>Phosphoric monoester hydrolases</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Protéines de liaison à l'ADN</term><term>Protéines de répression</term><term>Protéines fongiques</term><term>Protéines nucléaires</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sirolimus</term><term>Tacrolimus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sirolimus</term><term>Tacrolimus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Fluorescent Antibody Technique</term><term>Glutathione Peroxidase</term><term>Models, Genetic</term><term>Mutation</term><term>Phosphatidylinositol 3-Kinases</term><term>Phosphorylation</term><term>Prions</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Recombinant Fusion Proteins</term><term>Saccharomyces cerevisiae Proteins</term><term>Two-Hybrid System Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Glutathione peroxidase</term><term>Liaison aux protéines</term><term>Modèles génétiques</term><term>Mutation</term><term>Phosphatidylinositol 3-kinases</term><term>Phosphorylation</term><term>Prions</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de fusion recombinantes</term><term>Structure tertiaire des protéines</term><term>Technique d'immunofluorescence</term><term>Techniques de double hybride</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Gln3p is a GATA-type transcription factor responsive to different nitrogen nutrients and starvation in yeast Saccharomyces cerevisiae. Recent evidence has linked TOR signaling to Gln3p. Rapamycin causes dephosphorylation and nuclear translocation of Gln3p, thereby activating nitrogen catabolite repressible-sensitive genes. However, a detailed mechanistic understanding of this process is lacking. In this study, we show that Tor1p physically interacts with Gln3p. An intact TOR kinase domain is essential for the phosphorylation of Gln3p, inhibition of Gln3p nuclear entry and repression of Gln3p-dependent transcription. In contrast, at least two distinct protein phosphatases, Pph3p and the Tap42p-dependent phosphatases, are involved in the activation of Gln3p. The yeast pro-prion protein Ure2p binds to both hyper- and hypo-phosphorylated Gln3p. In contrast to the free Gln3p, the Ure2p-bound Gln3p is signifcantly resistant to dephosphorylation. Taken together, these results reveal a tripartite regulatory mechanism by which the phosphorylation of Gln3p is regulated.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10940301</PMID><DateCompleted><Year>2000</Year><Month>12</Month><Day>29</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>275</Volume><Issue>46</Issue><PubDate><Year>2000</Year><Month>Nov</Month><Day>17</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Tripartite regulation of Gln3p by TOR, Ure2p, and phosphatases.</ArticleTitle><Pagination><MedlinePgn>35727-33</MedlinePgn></Pagination><Abstract><AbstractText>Gln3p is a GATA-type transcription factor responsive to different nitrogen nutrients and starvation in yeast Saccharomyces cerevisiae. Recent evidence has linked TOR signaling to Gln3p. Rapamycin causes dephosphorylation and nuclear translocation of Gln3p, thereby activating nitrogen catabolite repressible-sensitive genes. However, a detailed mechanistic understanding of this process is lacking. In this study, we show that Tor1p physically interacts with Gln3p. An intact TOR kinase domain is essential for the phosphorylation of Gln3p, inhibition of Gln3p nuclear entry and repression of Gln3p-dependent transcription. In contrast, at least two distinct protein phosphatases, Pph3p and the Tap42p-dependent phosphatases, are involved in the activation of Gln3p. The yeast pro-prion protein Ure2p binds to both hyper- and hypo-phosphorylated Gln3p. In contrast to the free Gln3p, the Ure2p-bound Gln3p is signifcantly resistant to dephosphorylation. Taken together, these results reveal a tripartite regulatory mechanism by which the phosphorylation of Gln3p is regulated.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bertram</LastName><ForeName>P G</ForeName><Initials>PG</Initials><AffiliationInfo><Affiliation>Department of Pathology and Immunology and the Molecular Genetics and Molecular Cell Biology Programs, Washington University School of Medicine, St. Louis, Missouri 63110, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Choi</LastName><ForeName>J H</ForeName><Initials>JH</Initials></Author><Author ValidYN="Y"><LastName>Carvalho</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Ai</LastName><ForeName>W</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Zeng</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Chan</LastName><ForeName>T F</ForeName><Initials>TF</Initials></Author><Author ValidYN="Y"><LastName>Zheng</LastName><ForeName>X F</ForeName><Initials>XF</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C071664">GLN3 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009687">Nuclear Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011328">Prions</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012097">Repressor Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="D005979">Glutathione Peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="C067020">URE2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D019869">Phosphatidylinositol 3-Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D017853">Phosphotransferases (Alcohol Group Acceptor)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.137</RegistryNumber><NameOfSubstance UI="C083324">TOR1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.2</RegistryNumber><NameOfSubstance UI="D010744">Phosphoric Monoester Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical><Chemical><RegistryNumber>WM0HAQ4WNM</RegistryNumber><NameOfSubstance UI="D016559">Tacrolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005455" MajorTopicYN="N">Fluorescent Antibody Technique</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005979" MajorTopicYN="N">Glutathione Peroxidase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008957" MajorTopicYN="N">Models, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009687" MajorTopicYN="N">Nuclear Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019869" MajorTopicYN="Y">Phosphatidylinositol 3-Kinases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010744" MajorTopicYN="N">Phosphoric Monoester Hydrolases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017853" 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MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012097" MajorTopicYN="N">Repressor Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="Y">Saccharomyces cerevisiae Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016559" MajorTopicYN="N">Tacrolimus</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020798" MajorTopicYN="N">Two-Hybrid System Techniques</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>8</Month><Day>15</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>8</Month><Day>15</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10940301</ArticleId><ArticleId IdType="doi">10.1074/jbc.M004235200</ArticleId><ArticleId IdType="pii">M004235200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Missouri (État)</li></region><settlement><li>Saint-Louis (Missouri)</li></settlement><orgName><li>École de médecine (Université Washington de Saint-Louis)</li></orgName></list><tree><noCountry><name sortKey="Ai, W" sort="Ai, W" uniqKey="Ai W" first="W" last="Ai">W. Ai</name><name sortKey="Carvalho, J" sort="Carvalho, J" uniqKey="Carvalho J" first="J" last="Carvalho">J. Carvalho</name><name sortKey="Chan, T F" sort="Chan, T F" uniqKey="Chan T" first="T F" last="Chan">T F Chan</name><name sortKey="Choi, J H" sort="Choi, J H" uniqKey="Choi J" first="J H" last="Choi">J H Choi</name><name sortKey="Zeng, C" sort="Zeng, C" uniqKey="Zeng C" first="C" last="Zeng">C. Zeng</name><name sortKey="Zheng, X F" sort="Zheng, X F" uniqKey="Zheng X" first="X F" last="Zheng">X F Zheng</name></noCountry><country name="États-Unis"><region name="Missouri (État)"><name sortKey="Bertram, P G" sort="Bertram, P G" uniqKey="Bertram P" first="P G" last="Bertram">P G Bertram</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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