A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction.
Identifieur interne : 000578 ( Main/Exploration ); précédent : 000577; suivant : 000579A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction.
Auteurs : Cuiyun Hu ; Caifang Yu ; Yanhua Liu ; Xianhui Hou ; Xiaoyun Liu ; Yunfei Hu [République populaire de Chine] ; Changwen Jin [République populaire de Chine]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2015.
Descripteurs français
- KwdFr :
- Arsenate Reductases (composition chimique), Arsenate Reductases (génétique), Arsenate Reductases (métabolisme), Arséniates (composition chimique), Arséniates (métabolisme), Conformation des protéines (MeSH), Disulfures (métabolisme), Données de séquences moléculaires (MeSH), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glutathion (métabolisme), Modèles moléculaires (MeSH), Oxydoréduction (MeSH), Protéines bactériennes (composition chimique), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (MeSH), Structure secondaire des protéines (MeSH), Structure tertiaire des protéines (MeSH), Synechocystis (enzymologie), Synechocystis (génétique), Séquence d'acides aminés (MeSH), Thiols (métabolisme), Thiorédoxines (composition chimique), Thiorédoxines (génétique), Thiorédoxines (métabolisme).
- MESH :
- composition chimique : Arsenate Reductases, Arséniates, Glutarédoxines, Protéines bactériennes, Thiorédoxines.
- enzymologie : Synechocystis.
- génétique : Arsenate Reductases, Glutarédoxines, Protéines bactériennes, Synechocystis, Thiorédoxines.
- métabolisme : Arsenate Reductases, Arséniates, Disulfures, Glutarédoxines, Glutathion, Protéines bactériennes, Thiols, Thiorédoxines.
- Conformation des protéines, Données de séquences moléculaires, Modèles moléculaires, Oxydoréduction, Similitude de séquences d'acides aminés, Sites de fixation, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Arsenate Reductases (chemistry), Arsenate Reductases (genetics), Arsenate Reductases (metabolism), Arsenates (chemistry), Arsenates (metabolism), Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Binding Sites (MeSH), Disulfides (metabolism), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Protein Conformation (MeSH), Protein Structure, Secondary (MeSH), Protein Structure, Tertiary (MeSH), Sequence Homology, Amino Acid (MeSH), Sulfhydryl Compounds (metabolism), Synechocystis (enzymology), Synechocystis (genetics), Thioredoxins (chemistry), Thioredoxins (genetics), Thioredoxins (metabolism).
- MESH :
- chemical , chemistry : Arsenate Reductases, Arsenates, Bacterial Proteins, Glutaredoxins, Thioredoxins.
- chemical , genetics : Arsenate Reductases, Bacterial Proteins, Glutaredoxins, Thioredoxins.
- chemical , metabolism : Arsenate Reductases, Arsenates, Bacterial Proteins, Disulfides, Glutaredoxins, Glutathione, Sulfhydryl Compounds, Thioredoxins.
- enzymology : Synechocystis.
- genetics : Synechocystis.
- Amino Acid Sequence, Binding Sites, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid.
Abstract
Evolution of enzymes plays a crucial role in obtaining new biological functions for all life forms. Arsenate reductases (ArsC) are several families of arsenic detoxification enzymes that reduce arsenate to arsenite, which can subsequently be extruded from cells by specific transporters. Among these, the Synechocystis ArsC (SynArsC) is structurally homologous to the well characterized thioredoxin (Trx)-coupled ArsC family but requires the glutaredoxin (Grx) system for its reactivation, therefore classified as a unique Trx/Grx-hybrid family. The detailed catalytic mechanism of SynArsC is unclear and how the "hybrid" mechanism evolved remains enigmatic. Herein, we report the molecular mechanism of SynArsC by biochemical and structural studies. Our work demonstrates that arsenate reduction is carried out via an intramolecular thiol-disulfide cascade similar to the Trx-coupled family, whereas the enzyme reactivation step is diverted to the coupling of the glutathione-Grx pathway due to the local structural difference. The current results support the hypothesis that SynArsC is likely a molecular fossil representing an intermediate stage during the evolution of the Trx-coupled ArsC family from the low molecular weight protein phosphotyrosine phosphatase (LMW-PTPase) family.
DOI: 10.1074/jbc.M115.659896
PubMed: 26224634
PubMed Central: PMC4571977
Affiliations:
Links toward previous steps (curation, corpus...)
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last="Liu">Xiaoyun Liu</name><affiliation><nlm:affiliation>From the College of Chemistry and Molecular Engineering.</nlm:affiliation><wicri:noCountry code="no comma">From the College of Chemistry and Molecular Engineering.</wicri:noCountry></affiliation></author><author><name sortKey="Hu, Yunfei" sort="Hu, Yunfei" uniqKey="Hu Y" first="Yunfei" last="Hu">Yunfei Hu</name><affiliation wicri:level="1"><nlm:affiliation>From the College of Chemistry and Molecular Engineering, Beijing Nuclear Magnetic Resonance Center, yunfei@pku.edu.cn.</nlm:affiliation><country wicri:rule="url">République populaire de Chine</country><wicri:regionArea>From the College of Chemistry and Molecular Engineering, Beijing Nuclear Magnetic Resonance Center</wicri:regionArea><wicri:noRegion>Beijing Nuclear Magnetic Resonance Center</wicri:noRegion></affiliation></author><author><name sortKey="Jin, Changwen" sort="Jin, Changwen" uniqKey="Jin C" first="Changwen" last="Jin">Changwen Jin</name><affiliation wicri:level="4"><nlm:affiliation>From the College of Chemistry and Molecular Engineering, Beijing Nuclear Magnetic Resonance Center, College of Life Sciences, Beijing National Laboratory for Molecular Sciences, Peking University, Beijing 100871, China changwen@pku.edu.cn.</nlm:affiliation><country wicri:rule="url">République populaire de Chine</country><wicri:regionArea>From the College of Chemistry and Molecular Engineering, Beijing Nuclear Magnetic Resonance Center, College of Life Sciences, Beijing National Laboratory for Molecular Sciences, Peking University, Beijing 100871</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName><orgName type="university">Université de Pékin</orgName><placeName><settlement type="city">Pékin</settlement><region type="capitale">Pékin</region></placeName></affiliation></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2015" 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(MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Sulfhydryl Compounds (metabolism)</term><term>Synechocystis (enzymology)</term><term>Synechocystis (genetics)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (genetics)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arsenate Reductases (composition chimique)</term><term>Arsenate Reductases (génétique)</term><term>Arsenate Reductases (métabolisme)</term><term>Arséniates (composition chimique)</term><term>Arséniates (métabolisme)</term><term>Conformation des protéines (MeSH)</term><term>Disulfures (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines bactériennes (composition chimique)</term><term>Protéines bactériennes (génétique)</term><term>Protéines bactériennes (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Structure secondaire des protéines (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Synechocystis (enzymologie)</term><term>Synechocystis (génétique)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thiols (métabolisme)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Arsenate Reductases</term><term>Arsenates</term><term>Bacterial Proteins</term><term>Glutaredoxins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Arsenate Reductases</term><term>Bacterial 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Reductases</term><term>Glutarédoxines</term><term>Protéines bactériennes</term><term>Synechocystis</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arsenate Reductases</term><term>Arséniates</term><term>Disulfures</term><term>Glutarédoxines</term><term>Glutathion</term><term>Protéines bactériennes</term><term>Thiols</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Evolution of enzymes plays a crucial role in obtaining new biological functions for all life forms. Arsenate reductases (ArsC) are several families of arsenic detoxification enzymes that reduce arsenate to arsenite, which can subsequently be extruded from cells by specific transporters. Among these, the Synechocystis ArsC (SynArsC) is structurally homologous to the well characterized thioredoxin (Trx)-coupled ArsC family but requires the glutaredoxin (Grx) system for its reactivation, therefore classified as a unique Trx/Grx-hybrid family. The detailed catalytic mechanism of SynArsC is unclear and how the "hybrid" mechanism evolved remains enigmatic. Herein, we report the molecular mechanism of SynArsC by biochemical and structural studies. Our work demonstrates that arsenate reduction is carried out via an intramolecular thiol-disulfide cascade similar to the Trx-coupled family, whereas the enzyme reactivation step is diverted to the coupling of the glutathione-Grx pathway due to the local structural difference. The current results support the hypothesis that SynArsC is likely a molecular fossil representing an intermediate stage during the evolution of the Trx-coupled ArsC family from the low molecular weight protein phosphotyrosine phosphatase (LMW-PTPase) family. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26224634</PMID><DateCompleted><Year>2016</Year><Month>02</Month><Day>01</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>290</Volume><Issue>36</Issue><PubDate><Year>2015</Year><Month>Sep</Month><Day>04</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction.</ArticleTitle><Pagination><MedlinePgn>22262-73</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M115.659896</ELocationID><Abstract><AbstractText>Evolution of enzymes plays a crucial role in obtaining new biological functions for all life forms. Arsenate reductases (ArsC) are several families of arsenic detoxification enzymes that reduce arsenate to arsenite, which can subsequently be extruded from cells by specific transporters. Among these, the Synechocystis ArsC (SynArsC) is structurally homologous to the well characterized thioredoxin (Trx)-coupled ArsC family but requires the glutaredoxin (Grx) system for its reactivation, therefore classified as a unique Trx/Grx-hybrid family. The detailed catalytic mechanism of SynArsC is unclear and how the "hybrid" mechanism evolved remains enigmatic. Herein, we report the molecular mechanism of SynArsC by biochemical and structural studies. Our work demonstrates that arsenate reduction is carried out via an intramolecular thiol-disulfide cascade similar to the Trx-coupled family, whereas the enzyme reactivation step is diverted to the coupling of the glutathione-Grx pathway due to the local structural difference. The current results support the hypothesis that SynArsC is likely a molecular fossil representing an intermediate stage during the evolution of the Trx-coupled ArsC family from the low molecular weight protein phosphotyrosine phosphatase (LMW-PTPase) family. </AbstractText><CopyrightInformation>© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hu</LastName><ForeName>Cuiyun</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>From the College of Chemistry and Molecular Engineering, Beijing Nuclear Magnetic Resonance Center.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Caifang</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>From the College of Chemistry and Molecular Engineering, Beijing Nuclear Magnetic Resonance Center.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Yanhua</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>From the College of Chemistry and Molecular Engineering.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hou</LastName><ForeName>Xianhui</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>From the College of Chemistry and Molecular Engineering, Beijing Nuclear Magnetic Resonance Center.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Xiaoyun</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>From the College of Chemistry and Molecular Engineering.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hu</LastName><ForeName>Yunfei</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>From the College of Chemistry and Molecular Engineering, Beijing Nuclear Magnetic Resonance Center, yunfei@pku.edu.cn.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jin</LastName><ForeName>Changwen</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>From the College of Chemistry and Molecular Engineering, Beijing Nuclear Magnetic Resonance Center, College of Life Sciences, Beijing National Laboratory for Molecular Sciences, Peking University, Beijing 100871, China changwen@pku.edu.cn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>1JFV</AccessionNumber><AccessionNumber>1LJL</AccessionNumber><AccessionNumber>1LK0</AccessionNumber><AccessionNumber>1Z2E</AccessionNumber><AccessionNumber>2IPA</AccessionNumber><AccessionNumber>2MYN</AccessionNumber><AccessionNumber>2MYP</AccessionNumber><AccessionNumber>2MYT</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>07</Month><Day>29</Day></ArticleDate></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="D001149">Arsenates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.20.-</RegistryNumber><NameOfSubstance UI="D053502">Arsenate Reductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>N7CIZ75ZPN</RegistryNumber><NameOfSubstance UI="C025657">arsenic acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053502" MajorTopicYN="N">Arsenate Reductases</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="D001149" MajorTopicYN="N">Arsenates</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial 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="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName 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MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046939" MajorTopicYN="N">Synechocystis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">ArsC</Keyword><Keyword MajorTopicYN="N">SynArsC</Keyword><Keyword MajorTopicYN="N">arsenate reductase</Keyword><Keyword MajorTopicYN="N">arsenic detoxification</Keyword><Keyword MajorTopicYN="N">enzyme</Keyword><Keyword MajorTopicYN="N">enzyme catalysis</Keyword><Keyword MajorTopicYN="N">enzyme mechanism</Keyword><Keyword MajorTopicYN="N">nuclear magnetic resonance (NMR)</Keyword><Keyword MajorTopicYN="N">oxidation-reduction (redox)</Keyword><Keyword MajorTopicYN="N">protein structure</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>04</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>7</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>8</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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Hu</name><name sortKey="Liu, Xiaoyun" sort="Liu, Xiaoyun" uniqKey="Liu X" first="Xiaoyun" last="Liu">Xiaoyun Liu</name><name sortKey="Liu, Yanhua" sort="Liu, Yanhua" uniqKey="Liu Y" first="Yanhua" last="Liu">Yanhua Liu</name><name sortKey="Yu, Caifang" sort="Yu, Caifang" uniqKey="Yu C" first="Caifang" last="Yu">Caifang Yu</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Hu, Yunfei" sort="Hu, Yunfei" uniqKey="Hu Y" first="Yunfei" last="Hu">Yunfei Hu</name></noRegion><name sortKey="Jin, Changwen" sort="Jin, Changwen" uniqKey="Jin C" first="Changwen" last="Jin">Changwen Jin</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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