Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space.
Identifieur interne : 000539 ( Main/Exploration ); précédent : 000538; suivant : 000540Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space.
Auteurs : Kerstin Kojer [Allemagne] ; Valentina Peleh [Allemagne] ; Gaetano Calabrese [Allemagne] ; Johannes M. Herrmann [Allemagne] ; Jan Riemer [Allemagne]Source :
- Molecular biology of the cell [ 1939-4586 ] ; 2015.
Descripteurs français
- KwdFr :
- Chaperons moléculaires (génétique), Chaperons moléculaires (métabolisme), Cinétique (MeSH), Cytosol (métabolisme), Disulfure de glutathion (métabolisme), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glutathion (métabolisme), Immunotransfert (MeSH), Membranes mitochondriales (métabolisme), Metalloproteases (génétique), Metalloproteases (métabolisme), Mitochondries (métabolisme), Mutation (MeSH), Oxydoréduction (MeSH), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de transport de la membrane mitochondriale (génétique), Protéines de transport de la membrane mitochondriale (métabolisme), Protéines mitochondriales (MeSH), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Thiols (métabolisme), Transport des protéines (MeSH).
- MESH :
- génétique : Chaperons moléculaires, Glutarédoxines, Metalloproteases, Protéines de Saccharomyces cerevisiae, Protéines de transport de la membrane mitochondriale, Saccharomyces cerevisiae.
- métabolisme : Chaperons moléculaires, Cytosol, Disulfure de glutathion, Glutarédoxines, Glutathion, Membranes mitochondriales, Metalloproteases, Mitochondries, Protéines de Saccharomyces cerevisiae, Protéines de transport de la membrane mitochondriale, Saccharomyces cerevisiae, Thiols.
- Cinétique, Immunotransfert, Mutation, Oxydoréduction, Protéines mitochondriales, Transport des protéines.
English descriptors
- KwdEn :
- Cytosol (metabolism), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (metabolism), Glutathione Disulfide (metabolism), Immunoblotting (MeSH), Kinetics (MeSH), Metalloproteases (genetics), Metalloproteases (metabolism), Mitochondria (metabolism), Mitochondrial Membrane Transport Proteins (genetics), Mitochondrial Membrane Transport Proteins (metabolism), Mitochondrial Membranes (metabolism), Mitochondrial Proteins (MeSH), Molecular Chaperones (genetics), Molecular Chaperones (metabolism), Mutation (MeSH), Oxidation-Reduction (MeSH), Protein Transport (MeSH), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sulfhydryl Compounds (metabolism).
- MESH :
- chemical , genetics : Glutaredoxins, Metalloproteases, Mitochondrial Membrane Transport Proteins, Molecular Chaperones, Saccharomyces cerevisiae Proteins.
- genetics : Saccharomyces cerevisiae.
- metabolism : Cytosol, Glutaredoxins, Glutathione, Glutathione Disulfide, Metalloproteases, Mitochondria, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Molecular Chaperones, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sulfhydryl Compounds.
- Immunoblotting, Kinetics, Mitochondrial Proteins, Mutation, Oxidation-Reduction, Protein Transport.
Abstract
The mitochondrial intermembrane space (IMS) harbors an oxidizing machinery that drives import and folding of small cysteine-containing proteins without targeting signals. The main component of this pathway is the oxidoreductase Mia40, which introduces disulfides into its substrates. We recently showed that the IMS glutathione pool is maintained as reducing as that of the cytosol. It thus remained unclear how equilibration of protein disulfides with the IMS glutathione pool is prevented in order to allow oxidation-driven protein import. Here we demonstrate the presence of glutaredoxins in the IMS and show that limiting amounts of these glutaredoxins provide a kinetic barrier to prevent the thermodynamically feasible reduction of Mia40 substrates by the IMS glutathione pool. Moreover, they allow Mia40 to exist in a predominantly oxidized state. Consequently, overexpression of glutaredoxin 2 in the IMS results in a more reduced Mia40 redox state and a delay in oxidative folding and mitochondrial import of different Mia40 substrates. Our findings thus indicate that carefully balanced glutaredoxin amounts in the IMS ensure efficient oxidative folding in the reducing environment of this compartment.
DOI: 10.1091/mbc.E14-10-1422
PubMed: 25392302
PubMed Central: PMC4294668
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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(metabolism)</term><term>Mitochondrial Membranes (metabolism)</term><term>Mitochondrial Proteins (MeSH)</term><term>Molecular Chaperones (genetics)</term><term>Molecular Chaperones (metabolism)</term><term>Mutation (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Protein Transport (MeSH)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Sulfhydryl Compounds (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chaperons moléculaires (génétique)</term><term>Chaperons moléculaires (métabolisme)</term><term>Cinétique (MeSH)</term><term>Cytosol (métabolisme)</term><term>Disulfure de glutathion (métabolisme)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Immunotransfert (MeSH)</term><term>Membranes mitochondriales (métabolisme)</term><term>Metalloproteases (génétique)</term><term>Metalloproteases (métabolisme)</term><term>Mitochondries (métabolisme)</term><term>Mutation (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines de transport de la membrane mitochondriale (génétique)</term><term>Protéines de transport de la membrane mitochondriale (métabolisme)</term><term>Protéines mitochondriales (MeSH)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Thiols (métabolisme)</term><term>Transport des protéines (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Metalloproteases</term><term>Mitochondrial Membrane Transport Proteins</term><term>Molecular Chaperones</term><term>Saccharomyces cerevisiae 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drives import and folding of small cysteine-containing proteins without targeting signals. The main component of this pathway is the oxidoreductase Mia40, which introduces disulfides into its substrates. We recently showed that the IMS glutathione pool is maintained as reducing as that of the cytosol. It thus remained unclear how equilibration of protein disulfides with the IMS glutathione pool is prevented in order to allow oxidation-driven protein import. Here we demonstrate the presence of glutaredoxins in the IMS and show that limiting amounts of these glutaredoxins provide a kinetic barrier to prevent the thermodynamically feasible reduction of Mia40 substrates by the IMS glutathione pool. Moreover, they allow Mia40 to exist in a predominantly oxidized state. Consequently, overexpression of glutaredoxin 2 in the IMS results in a more reduced Mia40 redox state and a delay in oxidative folding and mitochondrial import of different Mia40 substrates. Our findings thus indicate that carefully balanced glutaredoxin amounts in the IMS ensure efficient oxidative folding in the reducing environment of this compartment. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25392302</PMID><DateCompleted><Year>2015</Year><Month>10</Month><Day>02</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1939-4586</ISSN><JournalIssue CitedMedium="Internet"><Volume>26</Volume><Issue>2</Issue><PubDate><Year>2015</Year><Month>Jan</Month><Day>15</Day></PubDate></JournalIssue><Title>Molecular biology of the cell</Title><ISOAbbreviation>Mol Biol Cell</ISOAbbreviation></Journal><ArticleTitle>Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space.</ArticleTitle><Pagination><MedlinePgn>195-204</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1091/mbc.E14-10-1422</ELocationID><Abstract><AbstractText>The mitochondrial intermembrane space (IMS) harbors an oxidizing machinery that drives import and folding of small cysteine-containing proteins without targeting signals. The main component of this pathway is the oxidoreductase Mia40, which introduces disulfides into its substrates. We recently showed that the IMS glutathione pool is maintained as reducing as that of the cytosol. It thus remained unclear how equilibration of protein disulfides with the IMS glutathione pool is prevented in order to allow oxidation-driven protein import. Here we demonstrate the presence of glutaredoxins in the IMS and show that limiting amounts of these glutaredoxins provide a kinetic barrier to prevent the thermodynamically feasible reduction of Mia40 substrates by the IMS glutathione pool. Moreover, they allow Mia40 to exist in a predominantly oxidized state. Consequently, overexpression of glutaredoxin 2 in the IMS results in a more reduced Mia40 redox state and a delay in oxidative folding and mitochondrial import of different Mia40 substrates. Our findings thus indicate that carefully balanced glutaredoxin amounts in the IMS ensure efficient oxidative folding in the reducing environment of this compartment. </AbstractText><CopyrightInformation>© 2015 Kojer et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kojer</LastName><ForeName>Kerstin</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Cellular Biochemistry, University of Kaiserslautern, 67663 Kaiserslautern, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Peleh</LastName><ForeName>Valentina</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Cell Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Calabrese</LastName><ForeName>Gaetano</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Cellular Biochemistry, University of Kaiserslautern, 67663 Kaiserslautern, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Herrmann</LastName><ForeName>Johannes M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Cell Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Riemer</LastName><ForeName>Jan</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Cellular Biochemistry, University of Kaiserslautern, 67663 Kaiserslautern, Germany jan.riemer@biologie.uni-kl.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>2014</Year><Month>11</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Biol Cell</MedlineTA><NlmUniqueID>9201390</NlmUniqueID><ISSNLinking>1059-1524</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C491960">CCS1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C527885">Grx2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C495320">MIA40 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D033681">Mitochondrial Membrane Transport 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="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="C519195">ATP23 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D045726">Metalloproteases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>ULW86O013H</RegistryNumber><NameOfSubstance UI="D019803">Glutathione Disulfide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019803" MajorTopicYN="N">Glutathione Disulfide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015151" MajorTopicYN="N">Immunoblotting</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045726" MajorTopicYN="N">Metalloproteases</DescriptorName><QualifierName UI="Q000235" 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