Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p.
Identifieur interne : 000F47 ( Main/Exploration ); précédent : 000F46; suivant : 000F48Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p.
Auteurs : Ulrich Mühlenhoff [Allemagne] ; Jana Gerber ; Nadine Richhardt ; Roland LillSource :
- The EMBO journal [ 0261-4189 ] ; 2003.
Descripteurs français
- KwdFr :
- Adrénodoxine (métabolisme), Chaperons moléculaires (métabolisme), Cytosol (métabolisme), Ferrosulfoprotéines (métabolisme), Mitochondries (métabolisme), Modèles biologiques (MeSH), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de liaison au fer (métabolisme), Protéines mitochondriales (MeSH), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (physiologie).
- MESH :
- croissance et développement : Saccharomyces cerevisiae.
- métabolisme : Adrénodoxine, Chaperons moléculaires, Cytosol, Ferrosulfoprotéines, Mitochondries, Protéines de Saccharomyces cerevisiae, Protéines de liaison au fer.
- physiologie : Saccharomyces cerevisiae.
- Modèles biologiques, Protéines mitochondriales.
English descriptors
- KwdEn :
- Adrenodoxin (metabolism), Cytosol (metabolism), Iron-Binding Proteins (metabolism), Iron-Sulfur Proteins (metabolism), Mitochondria (metabolism), Mitochondrial Proteins (MeSH), Models, Biological (MeSH), Molecular Chaperones (metabolism), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae (physiology), Saccharomyces cerevisiae Proteins (metabolism).
- MESH :
- chemical , metabolism : Adrenodoxin, Iron-Binding Proteins, Iron-Sulfur Proteins, Molecular Chaperones, Saccharomyces cerevisiae Proteins.
- growth & development : Saccharomyces cerevisiae.
- metabolism : Cytosol, Mitochondria.
- physiology : Saccharomyces cerevisiae.
- chemical : Mitochondrial Proteins, Models, Biological.
Abstract
The mitochondrial proteins Isu1p and Isu2p play an essential role in the maturation of cellular iron-sulfur (Fe/S) proteins in eukaryotes. By radiolabelling of yeast cells with 55Fe we demonstrate that Isu1p binds an oxygen-resistant non-chelatable Fe/S cluster providing in vivo evidence for a scaffolding function of Isu1p during Fe/S cluster assembly. Depletion of the cysteine desulfurase Nfs1p, the ferredoxin Yah1p or the yeast frataxin homologue Yfh1p by regulated gene expression causes a strong decrease in the de novo synthesis of Fe/S clusters on Isu1p. In contrast, depletion of the Hsp70 chaperone Ssq1p, its co-chaperone Jac1p or the glutaredoxin Grx5p markedly increased the amount of Fe/S clusters bound to Isu1p, even though these mitochondrial proteins are crucial for maturation of Fe/S proteins. Hence Ssq1p/Jac1p and Grx5p are required in a step after Fe/S cluster synthesis on Isu1p, for instance in dissociation of preassembled Fe/S clusters from Isu1p and/or their insertion into apoproteins. We propose a model that dissects Fe/S cluster biogenesis into two major steps and assigns its central components to one of these two steps.
DOI: 10.1093/emboj/cdg446
PubMed: 12970193
PubMed Central: PMC212715
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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cerevisiae</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytosol</term><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adrénodoxine</term><term>Chaperons moléculaires</term><term>Cytosol</term><term>Ferrosulfoprotéines</term><term>Mitochondries</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de liaison au fer</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Mitochondrial Proteins</term><term>Models, Biological</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Modèles biologiques</term><term>Protéines mitochondriales</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The mitochondrial proteins Isu1p and Isu2p play an essential role in the maturation of cellular iron-sulfur (Fe/S) proteins in eukaryotes. By radiolabelling of yeast cells with 55Fe we demonstrate that Isu1p binds an oxygen-resistant non-chelatable Fe/S cluster providing in vivo evidence for a scaffolding function of Isu1p during Fe/S cluster assembly. Depletion of the cysteine desulfurase Nfs1p, the ferredoxin Yah1p or the yeast frataxin homologue Yfh1p by regulated gene expression causes a strong decrease in the de novo synthesis of Fe/S clusters on Isu1p. In contrast, depletion of the Hsp70 chaperone Ssq1p, its co-chaperone Jac1p or the glutaredoxin Grx5p markedly increased the amount of Fe/S clusters bound to Isu1p, even though these mitochondrial proteins are crucial for maturation of Fe/S proteins. Hence Ssq1p/Jac1p and Grx5p are required in a step after Fe/S cluster synthesis on Isu1p, for instance in dissociation of preassembled Fe/S clusters from Isu1p and/or their insertion into apoproteins. We propose a model that dissects Fe/S cluster biogenesis into two major steps and assigns its central components to one of these two steps.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12970193</PMID><DateCompleted><Year>2003</Year><Month>10</Month><Day>30</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0261-4189</ISSN><JournalIssue CitedMedium="Print"><Volume>22</Volume><Issue>18</Issue><PubDate><Year>2003</Year><Month>Sep</Month><Day>15</Day></PubDate></JournalIssue><Title>The EMBO journal</Title><ISOAbbreviation>EMBO J</ISOAbbreviation></Journal><ArticleTitle>Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p.</ArticleTitle><Pagination><MedlinePgn>4815-25</MedlinePgn></Pagination><Abstract><AbstractText>The mitochondrial proteins Isu1p and Isu2p play an essential role in the maturation of cellular iron-sulfur (Fe/S) proteins in eukaryotes. By radiolabelling of yeast cells with 55Fe we demonstrate that Isu1p binds an oxygen-resistant non-chelatable Fe/S cluster providing in vivo evidence for a scaffolding function of Isu1p during Fe/S cluster assembly. Depletion of the cysteine desulfurase Nfs1p, the ferredoxin Yah1p or the yeast frataxin homologue Yfh1p by regulated gene expression causes a strong decrease in the de novo synthesis of Fe/S clusters on Isu1p. In contrast, depletion of the Hsp70 chaperone Ssq1p, its co-chaperone Jac1p or the glutaredoxin Grx5p markedly increased the amount of Fe/S clusters bound to Isu1p, even though these mitochondrial proteins are crucial for maturation of Fe/S proteins. Hence Ssq1p/Jac1p and Grx5p are required in a step after Fe/S cluster synthesis on Isu1p, for instance in dissociation of preassembled Fe/S clusters from Isu1p and/or their insertion into apoproteins. We propose a model that dissects Fe/S cluster biogenesis into two major steps and assigns its central components to one of these two steps.</AbstractText></Abstract><AuthorList CompleteYN="Y"><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, D-35033 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gerber</LastName><ForeName>Jana</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Richhardt</LastName><ForeName>Nadine</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Lill</LastName><ForeName>Roland</ForeName><Initials>R</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>EMBO J</MedlineTA><NlmUniqueID>8208664</NlmUniqueID><ISSNLinking>0261-4189</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C121520">ISU1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D033862">Iron-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024101">Mitochondrial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018832">Molecular Chaperones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C120375">YAH1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C098527">frataxin</NameOfSubstance></Chemical><Chemical><RegistryNumber>12687-22-8</RegistryNumber><NameOfSubstance UI="D000325">Adrenodoxin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000325" MajorTopicYN="N">Adrenodoxin</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="D033862" MajorTopicYN="N">Iron-Binding Proteins</DescriptorName><QualifierName UI="Q000378" 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