Glutaredoxins with iron-sulphur clusters in eukaryotes - Structure, function and impact on disease.
Identifieur interne : 000062 ( Main/Exploration ); précédent : 000061; suivant : 000063Glutaredoxins with iron-sulphur clusters in eukaryotes - Structure, function and impact on disease.
Auteurs : Carsten Berndt [Allemagne] ; Loïck Christ [France] ; Nicolas Rouhier [France] ; Ulrich Mühlenhoff [Allemagne]Source :
- Biochimica et biophysica acta. Bioenergetics [ 1879-2650 ] ; 2020.
Abstract
Among the thioredoxin superfamily of proteins, the observation that numerous glutaredoxins bind iron-sulphur (Fe/S) clusters is one of the more recent and major developments concerning their functional properties. Glutaredoxins are present in most organisms. All members of the class II subfamily (including most monothiol glutaredoxins), but also some members of the class I (mostly dithiol glutaredoxins) and class III (land plant-specific monothiol or dithiol glutaredoxins) are Fe/S proteins. In glutaredoxins characterised so far, the [2Fe2S] cluster is coordinated by two active-site cysteine residues and two molecules of non-covalently bound glutathione in homo-dimeric complexes bridged by the cluster. In contrast to dithiol glutaredoxins, monothiol glutaredoxins possess no or very little oxidoreductase activity, but have emerged as important players in cellular iron metabolism. In this review we summarise the recent developments of the most prominent Fe/S glutaredoxins in eukaryotes, the mitochondrial single domain monothiol glutaredoxin 5, the chloroplastic single domain monothiol glutaredoxin S14 and S16, the nuclear/cytosolic multi-domain monothiol glutaredoxin 3, and the mitochondrial/cytosolic dithiol glutaredoxin 2.
DOI: 10.1016/j.bbabio.2020.148317
PubMed: 32980338
Affiliations:
- Allemagne, France
- District de Düsseldorf, District de Giessen, Grand Est, Hesse (Land), Lorraine (région), Rhénanie-du-Nord-Westphalie
- Düsseldorf, Marbourg, Nancy
- Université de Lorraine
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In contrast to dithiol glutaredoxins, monothiol glutaredoxins possess no or very little oxidoreductase activity, but have emerged as important players in cellular iron metabolism. In this review we summarise the recent developments of the most prominent Fe/S glutaredoxins in eukaryotes, the mitochondrial single domain monothiol glutaredoxin 5, the chloroplastic single domain monothiol glutaredoxin S14 and S16, the nuclear/cytosolic multi-domain monothiol glutaredoxin 3, and the mitochondrial/cytosolic dithiol glutaredoxin 2.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">32980338</PMID><DateRevised><Year>2020</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-2650</ISSN><JournalIssue CitedMedium="Internet"><Volume>1862</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>Sep</Month><Day>24</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta. Bioenergetics</Title><ISOAbbreviation>Biochim Biophys Acta Bioenerg</ISOAbbreviation></Journal><ArticleTitle>Glutaredoxins with iron-sulphur clusters in eukaryotes - Structure, function and impact on disease.</ArticleTitle><Pagination><MedlinePgn>148317</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0005-2728(20)30167-5</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbabio.2020.148317</ELocationID><Abstract><AbstractText>Among the thioredoxin superfamily of proteins, the observation that numerous glutaredoxins bind iron-sulphur (Fe/S) clusters is one of the more recent and major developments concerning their functional properties. Glutaredoxins are present in most organisms. All members of the class II subfamily (including most monothiol glutaredoxins), but also some members of the class I (mostly dithiol glutaredoxins) and class III (land plant-specific monothiol or dithiol glutaredoxins) are Fe/S proteins. In glutaredoxins characterised so far, the [2Fe2S] cluster is coordinated by two active-site cysteine residues and two molecules of non-covalently bound glutathione in homo-dimeric complexes bridged by the cluster. In contrast to dithiol glutaredoxins, monothiol glutaredoxins possess no or very little oxidoreductase activity, but have emerged as important players in cellular iron metabolism. In this review we summarise the recent developments of the most prominent Fe/S glutaredoxins in eukaryotes, the mitochondrial single domain monothiol glutaredoxin 5, the chloroplastic single domain monothiol glutaredoxin S14 and S16, the nuclear/cytosolic multi-domain monothiol glutaredoxin 3, and the mitochondrial/cytosolic dithiol glutaredoxin 2.</AbstractText><CopyrightInformation>Copyright © 2020 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>Carsten</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Neurology, Medical Faculty, Heinrich-Heine University, Merowingerplatz1a, 40225 Düsseldorf, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Christ</LastName><ForeName>Loïck</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Université de Lorraine, INRAE, IAM, F-54000 Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Université de Lorraine, INRAE, IAM, F-54000 Nancy, France.</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 Str. 6, 35032 Marburg, Germany. Electronic address: muehlenh@staff.uni-marburg.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>09</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Bioenerg</MedlineTA><NlmUniqueID>101731706</NlmUniqueID><ISSNLinking>0005-2728</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Glutathione</Keyword><Keyword MajorTopicYN="N">Iron metabolism</Keyword><Keyword MajorTopicYN="N">Iron-sulphur cluster assembly</Keyword><Keyword MajorTopicYN="N">Mitochondria</Keyword><Keyword MajorTopicYN="N">Plastids</Keyword><Keyword MajorTopicYN="N">Redox control</Keyword></KeywordList><CoiStatement>Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>07</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>09</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>09</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>9</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>9</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>9</Month><Day>27</Day><Hour>20</Hour><Minute>23</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32980338</ArticleId><ArticleId IdType="pii">S0005-2728(20)30167-5</ArticleId><ArticleId IdType="doi">10.1016/j.bbabio.2020.148317</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li><li>France</li></country><region><li>District de Düsseldorf</li><li>District de Giessen</li><li>Grand Est</li><li>Hesse (Land)</li><li>Lorraine (région)</li><li>Rhénanie-du-Nord-Westphalie</li></region><settlement><li>Düsseldorf</li><li>Marbourg</li><li>Nancy</li></settlement><orgName><li>Université de Lorraine</li></orgName></list><tree><country name="Allemagne"><region name="Rhénanie-du-Nord-Westphalie"><name sortKey="Berndt, Carsten" sort="Berndt, Carsten" uniqKey="Berndt C" first="Carsten" last="Berndt">Carsten Berndt</name></region><name sortKey="Muhlenhoff, Ulrich" sort="Muhlenhoff, Ulrich" uniqKey="Muhlenhoff U" first="Ulrich" last="Mühlenhoff">Ulrich Mühlenhoff</name></country><country name="France"><region name="Grand Est"><name sortKey="Christ, Loick" sort="Christ, Loick" uniqKey="Christ L" first="Loïck" last="Christ">Loïck Christ</name></region><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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