GlutaredoxinV1, Main, Exploration, bibRecord, 000485

The role of mitochondria and the CIA machinery in the maturation of cytosolic and nuclear iron-sulfur proteins.

Identifieur interne : 000485 ( Main/Exploration ); précédent : 000484; suivant : 000486

The role of mitochondria and the CIA machinery in the maturation of cytosolic and nuclear iron-sulfur proteins.

Auteurs : Roland Lill [Allemagne] ; Rafal Dutkiewicz [Pologne] ; Sven A. Freibert [Allemagne] ; Torsten Heidenreich [Allemagne] ; Judita Mascarenhas [Allemagne] ; Daili J. Netz [Allemagne] ; Viktoria D. Paul [Allemagne] ; Antonio J. Pierik [Allemagne] ; Nadine Richter [Allemagne] ; Martin Stümpfig [Allemagne] ; Vasundara Srinivasan [Allemagne] ; Oliver Stehling [Allemagne] ; Ulrich Mühlenhoff [Allemagne]

Source :

European journal of cell biology [ 1618-1298 ]

RBID : pubmed:26099175

Descripteurs français

KwdFr :
- Cytosol (métabolisme), Ferrosulfoprotéines (métabolisme), Humains (MeSH), Mitochondries (métabolisme), Noyau de la cellule (métabolisme), Protéines de transport membranaire (métabolisme), Protéines mitochondriales (métabolisme), Transport des protéines (physiologie), Transporteurs ABC (métabolisme).
MESH :
- métabolisme : Cytosol, Ferrosulfoprotéines, Mitochondries, Noyau de la cellule, Protéines de transport membranaire, Protéines mitochondriales, Transporteurs ABC.
- physiologie : Transport des protéines.
- Humains.

English descriptors

KwdEn :
- ATP-Binding Cassette Transporters (metabolism), Cell Nucleus (metabolism), Cytosol (metabolism), Humans (MeSH), Iron-Sulfur Proteins (metabolism), Membrane Transport Proteins (metabolism), Mitochondria (metabolism), Mitochondrial Proteins (metabolism), Protein Transport (physiology).
MESH :
- chemical , metabolism : ATP-Binding Cassette Transporters, Iron-Sulfur Proteins, Membrane Transport Proteins, Mitochondrial Proteins.
- metabolism : Cell Nucleus, Cytosol, Mitochondria.
- physiology : Protein Transport.
- Humans.

Abstract

Mitochondria have been derived from alpha-bacterial endosymbionts during the evolution of eukaryotes. Numerous bacterial functions have been maintained inside the organelles including fatty acid degradation, citric acid cycle, oxidative phosphorylation, and the synthesis of heme or lipoic acid cofactors. Additionally, mitochondria have inherited the bacterial iron-sulfur cluster assembly (ISC) machinery. Many of the ISC components are essential for cell viability because they generate a still unknown, sulfur-containing compound for the assembly of cytosolic and nuclear Fe/S proteins that perform important functions in, e.g., protein translation, DNA synthesis and repair, and chromosome segregation. The sulfur-containing compound is exported by the mitochondrial ABC transporter Atm1 (human ABCB7) and utilized by components of the cytosolic iron-sulfur protein assembly (CIA) machinery. An appealing minimal model for the striking compartmentation of eukaryotic Fe/S protein biogenesis is provided by organisms that contain mitosomes instead of mitochondria. Mitosomes have been derived from mitochondria by reductive evolution, during which they have lost virtually all classical mitochondrial tasks. Nevertheless, mitosomes harbor all core ISC components which presumably have been maintained for assisting the maturation of cytosolic-nuclear Fe/S proteins. The current review is centered around the Atm1 export process. We present an overview on the mitochondrial requirements for the export reaction, summarize recent insights into the 3D structure and potential mechanism of Atm1, and explain how the CIA machinery uses the mitochondrial export product for the assembly of cytosolic and nuclear Fe/S proteins.

DOI: 10.1016/j.ejcb.2015.05.002
PubMed: 26099175

Affiliations:

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

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Le document en format XML

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<author><name sortKey="Muhlenhoff, Ulrich" sort="Muhlenhoff, Ulrich" uniqKey="Muhlenhoff U" first="Ulrich" last="Mühlenhoff">Ulrich Mühlenhoff</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">The role of mitochondria and the CIA machinery in the maturation of cytosolic and nuclear iron-sulfur proteins.</title>
<author><name sortKey="Lill, Roland" sort="Lill, Roland" uniqKey="Lill R" first="Roland" last="Lill">Roland Lill</name>
<affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans-Meerwein-Str. 6, 35043 Marburg, Germany. Electronic address: Lill@staff.uni-marburg.de.</nlm:affiliation>
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<wicri:regionArea>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans-Meerwein-Str. 6, 35043 Marburg</wicri:regionArea>
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<author><name sortKey="Paul, Viktoria D" sort="Paul, Viktoria D" uniqKey="Paul V" first="Viktoria D" last="Paul">Viktoria D. Paul</name>
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<wicri:regionArea>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg</wicri:regionArea>
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<region type="district" nuts="2">District de Giessen</region>
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<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, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg</wicri:regionArea>
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<region type="district" nuts="2">District de Giessen</region>
<settlement type="city">Marbourg</settlement>
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<author><name sortKey="Srinivasan, Vasundara" sort="Srinivasan, Vasundara" uniqKey="Srinivasan V" first="Vasundara" last="Srinivasan">Vasundara Srinivasan</name>
<affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans-Meerwein-Str. 6, 35043 Marburg, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans-Meerwein-Str. 6, 35043 Marburg</wicri:regionArea>
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<region type="district" nuts="2">District de Giessen</region>
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</author>
<author><name sortKey="Stehling, Oliver" sort="Stehling, Oliver" uniqKey="Stehling O" first="Oliver" last="Stehling">Oliver Stehling</name>
<affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 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, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 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>
</analytic>
<series><title level="j">European journal of cell biology</title>
<idno type="eISSN">1618-1298</idno>
</series>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ATP-Binding Cassette Transporters (metabolism)</term>
<term>Cell Nucleus (metabolism)</term>
<term>Cytosol (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Membrane Transport Proteins (metabolism)</term>
<term>Mitochondria (metabolism)</term>
<term>Mitochondrial Proteins (metabolism)</term>
<term>Protein Transport (physiology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cytosol (métabolisme)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Mitochondries (métabolisme)</term>
<term>Noyau de la cellule (métabolisme)</term>
<term>Protéines de transport membranaire (métabolisme)</term>
<term>Protéines mitochondriales (métabolisme)</term>
<term>Transport des protéines (physiologie)</term>
<term>Transporteurs ABC (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>ATP-Binding Cassette Transporters</term>
<term>Iron-Sulfur Proteins</term>
<term>Membrane Transport Proteins</term>
<term>Mitochondrial Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term>
<term>Cytosol</term>
<term>Mitochondria</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytosol</term>
<term>Ferrosulfoprotéines</term>
<term>Mitochondries</term>
<term>Noyau de la cellule</term>
<term>Protéines de transport membranaire</term>
<term>Protéines mitochondriales</term>
<term>Transporteurs ABC</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Transport des protéines</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Protein Transport</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Humans</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Humains</term>
</keywords>
</textClass>
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<front><div type="abstract" xml:lang="en">Mitochondria have been derived from alpha-bacterial endosymbionts during the evolution of eukaryotes. Numerous bacterial functions have been maintained inside the organelles including fatty acid degradation, citric acid cycle, oxidative phosphorylation, and the synthesis of heme or lipoic acid cofactors. Additionally, mitochondria have inherited the bacterial iron-sulfur cluster assembly (ISC) machinery. Many of the ISC components are essential for cell viability because they generate a still unknown, sulfur-containing compound for the assembly of cytosolic and nuclear Fe/S proteins that perform important functions in, e.g., protein translation, DNA synthesis and repair, and chromosome segregation. The sulfur-containing compound is exported by the mitochondrial ABC transporter Atm1 (human ABCB7) and utilized by components of the cytosolic iron-sulfur protein assembly (CIA) machinery. An appealing minimal model for the striking compartmentation of eukaryotic Fe/S protein biogenesis is provided by organisms that contain mitosomes instead of mitochondria. Mitosomes have been derived from mitochondria by reductive evolution, during which they have lost virtually all classical mitochondrial tasks. Nevertheless, mitosomes harbor all core ISC components which presumably have been maintained for assisting the maturation of cytosolic-nuclear Fe/S proteins. The current review is centered around the Atm1 export process. We present an overview on the mitochondrial requirements for the export reaction, summarize recent insights into the 3D structure and potential mechanism of Atm1, and explain how the CIA machinery uses the mitochondrial export product for the assembly of cytosolic and nuclear Fe/S proteins. </div>
</front>
</TEI>
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<DateCompleted><Year>2016</Year>
<Month>06</Month>
<Day>09</Day>
</DateCompleted>
<DateRevised><Year>2017</Year>
<Month>12</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1618-1298</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>94</Volume>
<Issue>7-9</Issue>
<PubDate><MedlineDate>2015 Jul-Sep</MedlineDate>
</PubDate>
</JournalIssue>
<Title>European journal of cell biology</Title>
<ISOAbbreviation>Eur J Cell Biol</ISOAbbreviation>
</Journal>
<ArticleTitle>The role of mitochondria and the CIA machinery in the maturation of cytosolic and nuclear iron-sulfur proteins.</ArticleTitle>
<Pagination><MedlinePgn>280-91</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ejcb.2015.05.002</ELocationID>
<ELocationID EIdType="pii" ValidYN="Y">S0171-9335(15)00048-5</ELocationID>
<Abstract><AbstractText>Mitochondria have been derived from alpha-bacterial endosymbionts during the evolution of eukaryotes. Numerous bacterial functions have been maintained inside the organelles including fatty acid degradation, citric acid cycle, oxidative phosphorylation, and the synthesis of heme or lipoic acid cofactors. Additionally, mitochondria have inherited the bacterial iron-sulfur cluster assembly (ISC) machinery. Many of the ISC components are essential for cell viability because they generate a still unknown, sulfur-containing compound for the assembly of cytosolic and nuclear Fe/S proteins that perform important functions in, e.g., protein translation, DNA synthesis and repair, and chromosome segregation. The sulfur-containing compound is exported by the mitochondrial ABC transporter Atm1 (human ABCB7) and utilized by components of the cytosolic iron-sulfur protein assembly (CIA) machinery. An appealing minimal model for the striking compartmentation of eukaryotic Fe/S protein biogenesis is provided by organisms that contain mitosomes instead of mitochondria. Mitosomes have been derived from mitochondria by reductive evolution, during which they have lost virtually all classical mitochondrial tasks. Nevertheless, mitosomes harbor all core ISC components which presumably have been maintained for assisting the maturation of cytosolic-nuclear Fe/S proteins. The current review is centered around the Atm1 export process. We present an overview on the mitochondrial requirements for the export reaction, summarize recent insights into the 3D structure and potential mechanism of Atm1, and explain how the CIA machinery uses the mitochondrial export product for the assembly of cytosolic and nuclear Fe/S proteins. </AbstractText>
<CopyrightInformation>Copyright © 2015 Elsevier GmbH. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lill</LastName>
<ForeName>Roland</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans-Meerwein-Str. 6, 35043 Marburg, Germany. Electronic address: Lill@staff.uni-marburg.de.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dutkiewicz</LastName>
<ForeName>Rafal</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; Department of Molecular and Cellular Biology, Faculty of Biotechnology, University of Gdansk, 80-822 Gdansk, Poland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Freibert</LastName>
<ForeName>Sven A</ForeName>
<Initials>SA</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans-Meerwein-Str. 6, 35043 Marburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Heidenreich</LastName>
<ForeName>Torsten</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Mascarenhas</LastName>
<ForeName>Judita</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans-Meerwein-Str. 6, 35043 Marburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Netz</LastName>
<ForeName>Daili J</ForeName>
<Initials>DJ</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Paul</LastName>
<ForeName>Viktoria D</ForeName>
<Initials>VD</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Pierik</LastName>
<ForeName>Antonio J</ForeName>
<Initials>AJ</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; Fachbereich Chemie, TU Kaiserslautern, Erwin-Schrödinger-Straße 54, 67663 Kaiserslautern, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Richter</LastName>
<ForeName>Nadine</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Stümpfig</LastName>
<ForeName>Martin</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Srinivasan</LastName>
<ForeName>Vasundara</ForeName>
<Initials>V</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans-Meerwein-Str. 6, 35043 Marburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Stehling</LastName>
<ForeName>Oliver</ForeName>
<Initials>O</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Mühlenhoff</LastName>
<ForeName>Ulrich</ForeName>
<Initials>U</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</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>
<PublicationType UI="D016454">Review</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2015</Year>
<Month>05</Month>
<Day>31</Day>
</ArticleDate>
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<MedlineJournalInfo><Country>Germany</Country>
<MedlineTA>Eur J Cell Biol</MedlineTA>
<NlmUniqueID>7906240</NlmUniqueID>
<ISSNLinking>0171-9335</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C113037">ABCB7 protein, human</NameOfSubstance>
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<Keyword MajorTopicYN="N">Cysteine desulfurase</Keyword>
<Keyword MajorTopicYN="N">Frataxin</Keyword>
<Keyword MajorTopicYN="N">Glutaredoxin</Keyword>
<Keyword MajorTopicYN="N">Glutathione</Keyword>
<Keyword MajorTopicYN="N">Iron storage disease</Keyword>
<Keyword MajorTopicYN="N">Iron–sulfur cluster</Keyword>
<Keyword MajorTopicYN="N">Membrane transport</Keyword>
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The role of mitochondria and the CIA machinery in the maturation of cytosolic and nuclear iron-sulfur proteins.

The role of mitochondria and the CIA machinery in the maturation of cytosolic and nuclear iron-sulfur proteins.

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