Depletion of thiol reducing capacity impairs cytosolic but not mitochondrial iron-sulfur protein assembly machineries.
Identifieur interne : 000177 ( Main/Exploration ); précédent : 000176; suivant : 000178Depletion of thiol reducing capacity impairs cytosolic but not mitochondrial iron-sulfur protein assembly machineries.
Auteurs : Joseph J. Braymer [Allemagne] ; Martin Stümpfig [Allemagne] ; Stefanie Thelen [Allemagne] ; Ulrich Mühlenhoff [Allemagne] ; Roland Lill [Allemagne]Source :
- Biochimica et biophysica acta. Molecular cell research [ 1879-2596 ] ; 2019.
Descripteurs français
- KwdFr :
- Cytosol (métabolisme), Fer (métabolisme), Ferrosulfoprotéines (biosynthèse), Ferrosulfoprotéines (génétique), Ferrosulfoprotéines (métabolisme), Glutarédoxines (métabolisme), Homéostasie (MeSH), Instabilité du génome (MeSH), Mitochondries (métabolisme), Noyau de la cellule (métabolisme), Oxydoréduction (MeSH), Protéines de Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (génétique), Soufre (métabolisme), Thiols (métabolisme), Thiorédoxines (métabolisme), Transport des protéines (MeSH).
- MESH :
- biosynthèse : Ferrosulfoprotéines.
- génétique : Ferrosulfoprotéines, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : Cytosol, Fer, Ferrosulfoprotéines, Glutarédoxines, Mitochondries, Noyau de la cellule, Soufre, Thiols, Thiorédoxines.
- Homéostasie, Instabilité du génome, Oxydoréduction, Transport des protéines.
English descriptors
- KwdEn :
- Cell Nucleus (metabolism), Cytosol (metabolism), Genomic Instability (MeSH), Glutaredoxins (metabolism), Homeostasis (MeSH), Iron (metabolism), Iron-Sulfur Proteins (biosynthesis), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (metabolism), Mitochondria (metabolism), Oxidation-Reduction (MeSH), Protein Transport (MeSH), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae Proteins (genetics), Sulfhydryl Compounds (metabolism), Sulfur (metabolism), Thioredoxins (metabolism).
- MESH :
- chemical , biosynthesis : Iron-Sulfur Proteins.
- chemical , genetics : Iron-Sulfur Proteins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Glutaredoxins, Iron, Iron-Sulfur Proteins, Sulfhydryl Compounds, Sulfur, Thioredoxins.
- genetics : Saccharomyces cerevisiae.
- metabolism : Cell Nucleus, Cytosol, Mitochondria.
- Genomic Instability, Homeostasis, Oxidation-Reduction, Protein Transport.
Abstract
Iron‑sulfur (Fe/S) clusters are versatile inorganic cofactors that play central roles in essential cellular functions, from respiration to genome stability. >30 proteins involved in Fe/S protein biogenesis in eukaryotes are known, many of which bind clusters via cysteine residues. This opens up the possibility that the thiol-reducing glutaredoxin and thioredoxin systems are required at both the Fe/S biogenesis and target protein level to counteract thiol oxidation. To address the possible interplay of thiol redox chemistry and Fe/S protein biogenesis, we have characterized the status of the mitochondrial (ISC) and cytosolic (CIA) Fe/S protein assembly machineries in Saccharomyces cerevisiae mutants in which the three partially redundant glutathione (Glr1) and thioredoxin (Trr1 and Trr2) oxidoreductases have been inactivated in either mitochondria, cytosol, or both compartments. Cells devoid of mitochondrial oxidoreductases maintained a functional mitochondrial ISC machinery and showed no altered iron homeostasis despite a non-functional complex II of the respiratory chain due to redox-specific defects. In cells that lack either cytosolic or total cellular thiol reducing capacity, both the ISC system and iron homeostasis were normal, yet cytosolic and nuclear Fe/S target proteins were not matured. This dysfunction could be attributed to a failure in the assembly of [4Fe‑4S] clusters in the CIA factor Nar1, even though Nar1 maintained robust protein levels and stable interactions with later-acting CIA components. Overall, our analysis has uncovered a hitherto unknown thiol-dependence of the CIA machinery and has demonstrated the surprisingly varying sensitivity of Fe/S proteins to thiol oxidation.
DOI: 10.1016/j.bbamcr.2018.11.003
PubMed: 30419257
Affiliations:
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Braymer</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author><author><name sortKey="Stumpfig, Martin" sort="Stumpfig, Martin" uniqKey="Stumpfig M" first="Martin" last="Stümpfig">Martin Stümpfig</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author><author><name sortKey="Thelen, Stefanie" sort="Thelen, Stefanie" uniqKey="Thelen S" first="Stefanie" last="Thelen">Stefanie Thelen</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author><author><name sortKey="Muhlenhoff, Ulrich" sort="Muhlenhoff, Ulrich" uniqKey="Muhlenhoff U" first="Ulrich" last="Mühlenhoff">Ulrich Mühlenhoff</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany. 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Electronic address: lill@staff.uni-marburg.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany; LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans-Meerwein-Str., 35043 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta. 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This opens up the possibility that the thiol-reducing glutaredoxin and thioredoxin systems are required at both the Fe/S biogenesis and target protein level to counteract thiol oxidation. To address the possible interplay of thiol redox chemistry and Fe/S protein biogenesis, we have characterized the status of the mitochondrial (ISC) and cytosolic (CIA) Fe/S protein assembly machineries in Saccharomyces cerevisiae mutants in which the three partially redundant glutathione (Glr1) and thioredoxin (Trr1 and Trr2) oxidoreductases have been inactivated in either mitochondria, cytosol, or both compartments. Cells devoid of mitochondrial oxidoreductases maintained a functional mitochondrial ISC machinery and showed no altered iron homeostasis despite a non-functional complex II of the respiratory chain due to redox-specific defects. In cells that lack either cytosolic or total cellular thiol reducing capacity, both the ISC system and iron homeostasis were normal, yet cytosolic and nuclear Fe/S target proteins were not matured. This dysfunction could be attributed to a failure in the assembly of [4Fe‑4S] clusters in the CIA factor Nar1, even though Nar1 maintained robust protein levels and stable interactions with later-acting CIA components. Overall, our analysis has uncovered a hitherto unknown thiol-dependence of the CIA machinery and has demonstrated the surprisingly varying sensitivity of Fe/S proteins to thiol oxidation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30419257</PMID><DateCompleted><Year>2019</Year><Month>09</Month><Day>03</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>03</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-2596</ISSN><JournalIssue CitedMedium="Internet"><Volume>1866</Volume><Issue>2</Issue><PubDate><Year>2019</Year><Month>02</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta. Molecular cell research</Title><ISOAbbreviation>Biochim Biophys Acta Mol Cell Res</ISOAbbreviation></Journal><ArticleTitle>Depletion of thiol reducing capacity impairs cytosolic but not mitochondrial iron-sulfur protein assembly machineries.</ArticleTitle><Pagination><MedlinePgn>240-251</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0167-4889(18)30335-5</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbamcr.2018.11.003</ELocationID><Abstract><AbstractText>Iron‑sulfur (Fe/S) clusters are versatile inorganic cofactors that play central roles in essential cellular functions, from respiration to genome stability. >30 proteins involved in Fe/S protein biogenesis in eukaryotes are known, many of which bind clusters via cysteine residues. This opens up the possibility that the thiol-reducing glutaredoxin and thioredoxin systems are required at both the Fe/S biogenesis and target protein level to counteract thiol oxidation. To address the possible interplay of thiol redox chemistry and Fe/S protein biogenesis, we have characterized the status of the mitochondrial (ISC) and cytosolic (CIA) Fe/S protein assembly machineries in Saccharomyces cerevisiae mutants in which the three partially redundant glutathione (Glr1) and thioredoxin (Trr1 and Trr2) oxidoreductases have been inactivated in either mitochondria, cytosol, or both compartments. Cells devoid of mitochondrial oxidoreductases maintained a functional mitochondrial ISC machinery and showed no altered iron homeostasis despite a non-functional complex II of the respiratory chain due to redox-specific defects. In cells that lack either cytosolic or total cellular thiol reducing capacity, both the ISC system and iron homeostasis were normal, yet cytosolic and nuclear Fe/S target proteins were not matured. This dysfunction could be attributed to a failure in the assembly of [4Fe‑4S] clusters in the CIA factor Nar1, even though Nar1 maintained robust protein levels and stable interactions with later-acting CIA components. Overall, our analysis has uncovered a hitherto unknown thiol-dependence of the CIA machinery and has demonstrated the surprisingly varying sensitivity of Fe/S proteins to thiol oxidation.</AbstractText><CopyrightInformation>Copyright © 2018 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Braymer</LastName><ForeName>Joseph J</ForeName><Initials>JJ</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Stümpfig</LastName><ForeName>Martin</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thelen</LastName><ForeName>Stefanie</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mühlenhoff</LastName><ForeName>Ulrich</ForeName><Initials>U</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany. Electronic address: muehlenh@staff.uni-marburg.de.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lill</LastName><ForeName>Roland</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany; LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans-Meerwein-Str., 35043 Marburg, Germany. Electronic address: lill@staff.uni-marburg.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>11</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Mol Cell Res</MedlineTA><NlmUniqueID>101731731</NlmUniqueID><ISSNLinking>0167-4889</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</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>70FD1KFU70</RegistryNumber><NameOfSubstance UI="D013455">Sulfur</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D042822" MajorTopicYN="N">Genomic Instability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006706" MajorTopicYN="N">Homeostasis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013455" MajorTopicYN="N">Sulfur</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Glutathione oxidoreductase</Keyword><Keyword MajorTopicYN="Y">Iron homeostasis</Keyword><Keyword MajorTopicYN="Y">Iron‑sulfur clusters</Keyword><Keyword MajorTopicYN="Y">Saccharomyces cerevisiae</Keyword><Keyword MajorTopicYN="Y">Thiol redox chemistry</Keyword><Keyword MajorTopicYN="Y">Thioredoxin oxidoreductase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>09</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>11</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>11</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>11</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>9</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>11</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30419257</ArticleId><ArticleId IdType="pii">S0167-4889(18)30335-5</ArticleId><ArticleId IdType="doi">10.1016/j.bbamcr.2018.11.003</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>District de Giessen</li><li>Hesse (Land)</li></region><settlement><li>Marbourg</li></settlement></list><tree><country name="Allemagne"><region name="Hesse (Land)"><name sortKey="Braymer, Joseph J" sort="Braymer, Joseph J" uniqKey="Braymer J" first="Joseph J" last="Braymer">Joseph J. Braymer</name></region><name sortKey="Lill, Roland" sort="Lill, Roland" uniqKey="Lill R" first="Roland" last="Lill">Roland Lill</name><name sortKey="Muhlenhoff, Ulrich" sort="Muhlenhoff, Ulrich" uniqKey="Muhlenhoff U" first="Ulrich" last="Mühlenhoff">Ulrich Mühlenhoff</name><name sortKey="Stumpfig, Martin" sort="Stumpfig, Martin" uniqKey="Stumpfig M" first="Martin" last="Stümpfig">Martin Stümpfig</name><name sortKey="Thelen, Stefanie" sort="Thelen, Stefanie" uniqKey="Thelen S" first="Stefanie" last="Thelen">Stefanie Thelen</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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