An unusual mode of iron-sulfur-cluster coordination in a teleost glutaredoxin.
Identifieur interne : 000785 ( Main/Exploration ); précédent : 000784; suivant : 000786An unusual mode of iron-sulfur-cluster coordination in a teleost glutaredoxin.
Auteurs : Lars Br Utigam [Suède] ; Catrine Johansson ; Bastian Kubsch ; Michael A. Mcdonough ; Eckhard Bill ; Arne Holmgren ; Carsten BerndtSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2013.
Descripteurs français
- KwdFr :
- Activation enzymatique (MeSH), Animaux (MeSH), Cystéine (composition chimique), Danio zébré (métabolisme), Domaine catalytique (MeSH), Données de séquences moléculaires (MeSH), Ferrosulfoprotéines (composition chimique), Glutarédoxines (composition chimique), Humains (MeSH), Liaison aux protéines (MeSH), Ligands (MeSH), Motifs d'acides aminés (MeSH), Multimérisation de protéines (MeSH), Protéines de poisson-zèbre (composition chimique), Similitude de séquences d'acides aminés (MeSH).
- MESH :
- composition chimique : Cystéine, Ferrosulfoprotéines, Glutarédoxines, Protéines de poisson-zèbre.
- métabolisme : Danio zébré.
- Activation enzymatique, Animaux, Domaine catalytique, Données de séquences moléculaires, Humains, Liaison aux protéines, Ligands, Motifs d'acides aminés, Multimérisation de protéines, Similitude de séquences d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Animals (MeSH), Catalytic Domain (MeSH), Cysteine (chemistry), Enzyme Activation (MeSH), Glutaredoxins (chemistry), Humans (MeSH), Iron-Sulfur Proteins (chemistry), Ligands (MeSH), Molecular Sequence Data (MeSH), Protein Binding (MeSH), Protein Multimerization (MeSH), Sequence Homology, Amino Acid (MeSH), Zebrafish (metabolism), Zebrafish Proteins (chemistry).
- MESH :
- chemical , chemistry : Cysteine, Glutaredoxins, Iron-Sulfur Proteins, Zebrafish Proteins.
- metabolism : Zebrafish.
- Amino Acid Motifs, Animals, Catalytic Domain, Enzyme Activation, Humans, Ligands, Molecular Sequence Data, Protein Binding, Protein Multimerization, Sequence Homology, Amino Acid.
Abstract
Glutaredoxins that contain a Cys-X-X-Cys active site motif are glutathione-dependent thiol-disulfide oxidoreductases. Vertebrate glutaredoxin 2 is characterized by two extra cysteines that form an intra-molecular disulfide bridge. Zebrafish glutaredoxin 2 contains four additional cysteines that are conserved within the infraclass of bony fish (teleosts). Here, we present a biochemical and biophysical characterization of zebrafish glutaredoxin 2, focusing on iron-sulfur-cluster coordination. The coordination of [2Fe2S](2+)-clusters in monomers of this protein was revealed by both absorption and Mössbauer spectroscopy as well as size exclusion chromatography. All other holo-glutaredoxins represent [FeS]-cluster bridged dimers using two molecules of non-covalently bound glutathione and the N-terminal active site cysteines as ligands. These cysteine residues were not required for [FeS]-cluster coordination in zebrafish glutaredoxin 2. A crystal structure of the teleost protein revealed high structural similarity to its human homologue. The two vertebrate-specific cysteines as well as two of the teleost-specific cysteines are positioned within a radius of 7Å near the C-terminus suggesting a potential role in [FeS]-cluster coordination. Indeed, mutated proteins lacking these teleost-specific cysteines lost the ability to bind the cofactor. Hence, the apparent mode of [FeS]-cluster coordination in zebrafish glutaredoxin 2 could be different from all yet described [FeS]-glutaredoxins.
DOI: 10.1016/j.bbrc.2013.05.132
PubMed: 23756812
Affiliations:
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Mcdonough</name></author><author><name sortKey="Bill, Eckhard" sort="Bill, Eckhard" uniqKey="Bill E" first="Eckhard" last="Bill">Eckhard Bill</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author><author><name sortKey="Berndt, Carsten" sort="Berndt, Carsten" uniqKey="Berndt C" first="Carsten" last="Berndt">Carsten Berndt</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (MeSH)</term><term>Animals (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Cysteine (chemistry)</term><term>Enzyme Activation (MeSH)</term><term>Glutaredoxins (chemistry)</term><term>Humans (MeSH)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Ligands (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Protein Binding (MeSH)</term><term>Protein Multimerization (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Zebrafish (metabolism)</term><term>Zebrafish Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (MeSH)</term><term>Animaux (MeSH)</term><term>Cystéine (composition chimique)</term><term>Danio zébré (métabolisme)</term><term>Domaine catalytique (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Glutarédoxines (composition chimique)</term><term>Humains (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Ligands (MeSH)</term><term>Motifs d'acides aminés (MeSH)</term><term>Multimérisation de protéines (MeSH)</term><term>Protéines de poisson-zèbre (composition chimique)</term><term>Similitude de séquences d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Glutaredoxins</term><term>Iron-Sulfur Proteins</term><term>Zebrafish Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term><term>Ferrosulfoprotéines</term><term>Glutarédoxines</term><term>Protéines de poisson-zèbre</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Zebrafish</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Danio zébré</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Animals</term><term>Catalytic Domain</term><term>Enzyme Activation</term><term>Humans</term><term>Ligands</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Multimerization</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term><term>Animaux</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Liaison aux protéines</term><term>Ligands</term><term>Motifs d'acides aminés</term><term>Multimérisation de protéines</term><term>Similitude de séquences d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins that contain a Cys-X-X-Cys active site motif are glutathione-dependent thiol-disulfide oxidoreductases. Vertebrate glutaredoxin 2 is characterized by two extra cysteines that form an intra-molecular disulfide bridge. Zebrafish glutaredoxin 2 contains four additional cysteines that are conserved within the infraclass of bony fish (teleosts). Here, we present a biochemical and biophysical characterization of zebrafish glutaredoxin 2, focusing on iron-sulfur-cluster coordination. The coordination of [2Fe2S](2+)-clusters in monomers of this protein was revealed by both absorption and Mössbauer spectroscopy as well as size exclusion chromatography. All other holo-glutaredoxins represent [FeS]-cluster bridged dimers using two molecules of non-covalently bound glutathione and the N-terminal active site cysteines as ligands. These cysteine residues were not required for [FeS]-cluster coordination in zebrafish glutaredoxin 2. A crystal structure of the teleost protein revealed high structural similarity to its human homologue. The two vertebrate-specific cysteines as well as two of the teleost-specific cysteines are positioned within a radius of 7Å near the C-terminus suggesting a potential role in [FeS]-cluster coordination. Indeed, mutated proteins lacking these teleost-specific cysteines lost the ability to bind the cofactor. Hence, the apparent mode of [FeS]-cluster coordination in zebrafish glutaredoxin 2 could be different from all yet described [FeS]-glutaredoxins. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23756812</PMID><DateCompleted><Year>2013</Year><Month>09</Month><Day>09</Day></DateCompleted><DateRevised><Year>2018</Year><Month>04</Month><Day>29</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>436</Volume><Issue>3</Issue><PubDate><Year>2013</Year><Month>Jul</Month><Day>05</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>An unusual mode of iron-sulfur-cluster coordination in a teleost glutaredoxin.</ArticleTitle><Pagination><MedlinePgn>491-6</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2013.05.132</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0006-291X(13)00950-9</ELocationID><Abstract><AbstractText>Glutaredoxins that contain a Cys-X-X-Cys active site motif are glutathione-dependent thiol-disulfide oxidoreductases. Vertebrate glutaredoxin 2 is characterized by two extra cysteines that form an intra-molecular disulfide bridge. Zebrafish glutaredoxin 2 contains four additional cysteines that are conserved within the infraclass of bony fish (teleosts). Here, we present a biochemical and biophysical characterization of zebrafish glutaredoxin 2, focusing on iron-sulfur-cluster coordination. The coordination of [2Fe2S](2+)-clusters in monomers of this protein was revealed by both absorption and Mössbauer spectroscopy as well as size exclusion chromatography. All other holo-glutaredoxins represent [FeS]-cluster bridged dimers using two molecules of non-covalently bound glutathione and the N-terminal active site cysteines as ligands. These cysteine residues were not required for [FeS]-cluster coordination in zebrafish glutaredoxin 2. A crystal structure of the teleost protein revealed high structural similarity to its human homologue. The two vertebrate-specific cysteines as well as two of the teleost-specific cysteines are positioned within a radius of 7Å near the C-terminus suggesting a potential role in [FeS]-cluster coordination. Indeed, mutated proteins lacking these teleost-specific cysteines lost the ability to bind the cofactor. Hence, the apparent mode of [FeS]-cluster coordination in zebrafish glutaredoxin 2 could be different from all yet described [FeS]-glutaredoxins. </AbstractText><CopyrightInformation>Copyright © 2013 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bräutigam</LastName><ForeName>Lars</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Division for Biochemistry, Department for Medical Biochemistry and Biophysics, Karolinska Institutet, 17177 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Johansson</LastName><ForeName>Catrine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Kubsch</LastName><ForeName>Bastian</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>McDonough</LastName><ForeName>Michael A</ForeName><Initials>MA</Initials></Author><Author ValidYN="Y"><LastName>Bill</LastName><ForeName>Eckhard</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>Arne</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>Carsten</ForeName><Initials>C</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>092809</GrantID><Agency>Wellcome Trust</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>06</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</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="D008024">Ligands</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029961">Zebrafish Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008024" MajorTopicYN="N">Ligands</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015027" MajorTopicYN="N">Zebrafish</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029961" MajorTopicYN="N">Zebrafish Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Crystal structure</Keyword><Keyword MajorTopicYN="N">GSH</Keyword><Keyword MajorTopicYN="N">GSSG</Keyword><Keyword MajorTopicYN="N">Glutathione</Keyword><Keyword MajorTopicYN="N">Grx</Keyword><Keyword MajorTopicYN="N">HED</Keyword><Keyword MajorTopicYN="N">Mössbauer spectroscopy</Keyword><Keyword MajorTopicYN="N">Redox</Keyword><Keyword MajorTopicYN="N">Trx</Keyword><Keyword MajorTopicYN="N">Zebrafish</Keyword><Keyword MajorTopicYN="N">glutaredoxin</Keyword><Keyword MajorTopicYN="N">glutathion</Keyword><Keyword MajorTopicYN="N">glutathione disulphide</Keyword><Keyword MajorTopicYN="N">hydroxyethyl disulphide</Keyword><Keyword MajorTopicYN="N">thioredoxin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>05</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>05</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>6</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>6</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>9</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23756812</ArticleId><ArticleId IdType="pii">S0006-291X(13)00950-9</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2013.05.132</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country><region><li>Svealand</li></region><settlement><li>Stockholm</li></settlement></list><tree><noCountry><name sortKey="Berndt, Carsten" sort="Berndt, Carsten" uniqKey="Berndt C" first="Carsten" last="Berndt">Carsten Berndt</name><name sortKey="Bill, Eckhard" sort="Bill, Eckhard" uniqKey="Bill E" first="Eckhard" last="Bill">Eckhard Bill</name><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name><name sortKey="Johansson, Catrine" sort="Johansson, Catrine" uniqKey="Johansson C" first="Catrine" last="Johansson">Catrine Johansson</name><name sortKey="Kubsch, Bastian" sort="Kubsch, Bastian" uniqKey="Kubsch B" first="Bastian" last="Kubsch">Bastian Kubsch</name><name sortKey="Mcdonough, Michael A" sort="Mcdonough, Michael A" uniqKey="Mcdonough M" first="Michael A" last="Mcdonough">Michael A. Mcdonough</name></noCountry><country name="Suède"><region name="Svealand"><name sortKey="Br Utigam, Lars" sort="Br Utigam, Lars" uniqKey="Br Utigam L" first="Lars" last="Br Utigam">Lars Br Utigam</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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