CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster.
Identifieur interne : 000C96 ( Main/Exploration ); précédent : 000C95; suivant : 000C97CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster.
Auteurs : Antoine Picciocchi [France] ; Cyril Saguez ; Alain Boussac ; Corinne Cassier-Chauvat ; Franck ChauvatSource :
- Biochemistry [ 0006-2960 ] ; 2007.
Descripteurs français
- KwdFr :
- Acides aminés (génétique), Acides aminés (métabolisme), Alignement de séquences (MeSH), Cystéine (métabolisme), Données de séquences moléculaires (MeSH), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (métabolisme), Glutarédoxines (classification), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glutathion (composition chimique), Glutathion (métabolisme), Humains (MeSH), Ligands (MeSH), Modèles moléculaires (MeSH), Structure tertiaire des protéines (MeSH), Synechocystis (enzymologie), Synechocystis (génétique), Séquence conservée (MeSH), Séquence d'acides aminés (MeSH), Thiols (MeSH), Évolution moléculaire (MeSH).
- MESH :
- classification : Glutarédoxines.
- composition chimique : Ferrosulfoprotéines, Glutarédoxines, Glutathion.
- enzymologie : Synechocystis.
- génétique : Acides aminés, Glutarédoxines, Synechocystis.
- métabolisme : Acides aminés, Cystéine, Ferrosulfoprotéines, Glutarédoxines, Glutathion.
- Alignement de séquences, Données de séquences moléculaires, Humains, Ligands, Modèles moléculaires, Structure tertiaire des protéines, Séquence conservée, Séquence d'acides aminés, Thiols, Évolution moléculaire.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Amino Acids (genetics), Amino Acids (metabolism), Conserved Sequence (MeSH), Cysteine (metabolism), Evolution, Molecular (MeSH), Glutaredoxins (chemistry), Glutaredoxins (classification), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (chemistry), Glutathione (metabolism), Humans (MeSH), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Ligands (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Protein Structure, Tertiary (MeSH), Sequence Alignment (MeSH), Sulfhydryl Compounds (MeSH), Synechocystis (enzymology), Synechocystis (genetics).
- MESH :
- chemical , chemistry : Glutaredoxins, Glutathione, Iron-Sulfur Proteins.
- chemical , classification : Glutaredoxins.
- chemical , genetics : Amino Acids, Glutaredoxins.
- chemical , metabolism : Amino Acids, Cysteine, Glutaredoxins, Glutathione, Iron-Sulfur Proteins.
- enzymology : Synechocystis.
- genetics : Synechocystis.
- Amino Acid Sequence, Conserved Sequence, Evolution, Molecular, Humans, Ligands, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Sequence Alignment, Sulfhydryl Compounds.
Abstract
When produced in Escherichia coli, the CGFS-type monothiol Grxs from this organism (EcGrx4p) and the model cyanobacterium Synechocystis (SyGrx3p) exist as a dimeric iron-sulfur containing holoprotein or as a monomeric apoprotein in solution. Spectroscopic and site-directed mutagenesis analyses show that the SyGrx3 holoprotein contains a subunit-bridging [2Fe-2S] cluster that is ligated by the catalytic cysteine located in the CGFS motif of each monomer and the cysteines of two molecules of glutathione. The biochemical characterization of several monothiol Grxs from the cyanobacteria Gloeobacter violaceus (GvGrx3p) and Thermosynechococcus elongatus (TeGrx3p), the yeast Saccharomyces cerevisiae (ScGrx3p, ScGrx4p, and ScGrx5p), the plant Arabidopsis thaliana (AtGrx5p), and human (HsGrx5p) indicate that the incorporation of a GSH-ligated [2Fe-2S] center is a common feature of prokaryotic and eukaryotic CGFS-active site monothiol Grxs. In light of these results, the involvement of these enzymes in the sensing of iron and/or the biogenesis and transfer of Fe-S cluster is discussed.
DOI: 10.1021/bi7013272
PubMed: 18044966
Affiliations:
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sortKey="Boussac, Alain" sort="Boussac, Alain" uniqKey="Boussac A" first="Alain" last="Boussac">Alain Boussac</name></author><author><name sortKey="Cassier Chauvat, Corinne" sort="Cassier Chauvat, Corinne" uniqKey="Cassier Chauvat C" first="Corinne" last="Cassier-Chauvat">Corinne Cassier-Chauvat</name></author><author><name sortKey="Chauvat, Franck" sort="Chauvat, Franck" uniqKey="Chauvat F" first="Franck" last="Chauvat">Franck Chauvat</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:18044966</idno><idno type="pmid">18044966</idno><idno type="doi">10.1021/bi7013272</idno><idno type="wicri:Area/Main/Corpus">000C30</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C30</idno><idno type="wicri:Area/Main/Curation">000C30</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C30</idno><idno 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last="Saguez">Cyril Saguez</name></author><author><name sortKey="Boussac, Alain" sort="Boussac, Alain" uniqKey="Boussac A" first="Alain" last="Boussac">Alain Boussac</name></author><author><name sortKey="Cassier Chauvat, Corinne" sort="Cassier Chauvat, Corinne" uniqKey="Cassier Chauvat C" first="Corinne" last="Cassier-Chauvat">Corinne Cassier-Chauvat</name></author><author><name sortKey="Chauvat, Franck" sort="Chauvat, Franck" uniqKey="Chauvat F" first="Franck" last="Chauvat">Franck Chauvat</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Amino Acids (genetics)</term><term>Amino Acids (metabolism)</term><term>Conserved Sequence (MeSH)</term><term>Cysteine (metabolism)</term><term>Evolution, Molecular (MeSH)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (classification)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (chemistry)</term><term>Glutathione (metabolism)</term><term>Humans (MeSH)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Ligands (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Sequence Alignment (MeSH)</term><term>Sulfhydryl Compounds (MeSH)</term><term>Synechocystis (enzymology)</term><term>Synechocystis (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (génétique)</term><term>Acides aminés (métabolisme)</term><term>Alignement de séquences (MeSH)</term><term>Cystéine (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Glutarédoxines (classification)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (composition chimique)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Ligands (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Synechocystis (enzymologie)</term><term>Synechocystis (génétique)</term><term>Séquence conservée (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thiols (MeSH)</term><term>Évolution moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term><term>Glutathione</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Amino Acids</term><term>Glutaredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acids</term><term>Cysteine</term><term>Glutaredoxins</term><term>Glutathione</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Ferrosulfoprotéines</term><term>Glutarédoxines</term><term>Glutathion</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Synechocystis</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Synechocystis</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Synechocystis</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Acides aminés</term><term>Glutarédoxines</term><term>Synechocystis</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides aminés</term><term>Cystéine</term><term>Ferrosulfoprotéines</term><term>Glutarédoxines</term><term>Glutathion</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Conserved Sequence</term><term>Evolution, Molecular</term><term>Humans</term><term>Ligands</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Structure, Tertiary</term><term>Sequence Alignment</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Ligands</term><term>Modèles moléculaires</term><term>Structure tertiaire des protéines</term><term>Séquence conservée</term><term>Séquence d'acides aminés</term><term>Thiols</term><term>Évolution moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">When produced in Escherichia coli, the CGFS-type monothiol Grxs from this organism (EcGrx4p) and the model cyanobacterium Synechocystis (SyGrx3p) exist as a dimeric iron-sulfur containing holoprotein or as a monomeric apoprotein in solution. Spectroscopic and site-directed mutagenesis analyses show that the SyGrx3 holoprotein contains a subunit-bridging [2Fe-2S] cluster that is ligated by the catalytic cysteine located in the CGFS motif of each monomer and the cysteines of two molecules of glutathione. The biochemical characterization of several monothiol Grxs from the cyanobacteria Gloeobacter violaceus (GvGrx3p) and Thermosynechococcus elongatus (TeGrx3p), the yeast Saccharomyces cerevisiae (ScGrx3p, ScGrx4p, and ScGrx5p), the plant Arabidopsis thaliana (AtGrx5p), and human (HsGrx5p) indicate that the incorporation of a GSH-ligated [2Fe-2S] center is a common feature of prokaryotic and eukaryotic CGFS-active site monothiol Grxs. In light of these results, the involvement of these enzymes in the sensing of iron and/or the biogenesis and transfer of Fe-S cluster is discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18044966</PMID><DateCompleted><Year>2008</Year><Month>02</Month><Day>27</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>46</Volume><Issue>51</Issue><PubDate><Year>2007</Year><Month>Dec</Month><Day>25</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster.</ArticleTitle><Pagination><MedlinePgn>15018-26</MedlinePgn></Pagination><Abstract><AbstractText>When produced in Escherichia coli, the CGFS-type monothiol Grxs from this organism (EcGrx4p) and the model cyanobacterium Synechocystis (SyGrx3p) exist as a dimeric iron-sulfur containing holoprotein or as a monomeric apoprotein in solution. Spectroscopic and site-directed mutagenesis analyses show that the SyGrx3 holoprotein contains a subunit-bridging [2Fe-2S] cluster that is ligated by the catalytic cysteine located in the CGFS motif of each monomer and the cysteines of two molecules of glutathione. The biochemical characterization of several monothiol Grxs from the cyanobacteria Gloeobacter violaceus (GvGrx3p) and Thermosynechococcus elongatus (TeGrx3p), the yeast Saccharomyces cerevisiae (ScGrx3p, ScGrx4p, and ScGrx5p), the plant Arabidopsis thaliana (AtGrx5p), and human (HsGrx5p) indicate that the incorporation of a GSH-ligated [2Fe-2S] center is a common feature of prokaryotic and eukaryotic CGFS-active site monothiol Grxs. In light of these results, the involvement of these enzymes in the sensing of iron and/or the biogenesis and transfer of Fe-S cluster is discussed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Picciocchi</LastName><ForeName>Antoine</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>CEA, iBiTec-S, SBIGeM, LBI, Bat 142 CEA-Saclay, F-91191 Gif sur Yvette CEDEX, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Saguez</LastName><ForeName>Cyril</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Boussac</LastName><ForeName>Alain</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Cassier-Chauvat</LastName><ForeName>Corinne</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Chauvat</LastName><ForeName>Franck</ForeName><Initials>F</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><ArticleDate DateType="Electronic"><Year>2007</Year><Month>11</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><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="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019143" MajorTopicYN="N">Evolution, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName><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="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</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><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008024" MajorTopicYN="N">Ligands</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046939" MajorTopicYN="N">Synechocystis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>11</Month><Day>30</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>2</Month><Day>28</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>11</Month><Day>30</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18044966</ArticleId><ArticleId IdType="doi">10.1021/bi7013272</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Gif-sur-Yvette</li></settlement></list><tree><noCountry><name sortKey="Boussac, Alain" sort="Boussac, Alain" uniqKey="Boussac A" first="Alain" last="Boussac">Alain Boussac</name><name sortKey="Cassier Chauvat, Corinne" sort="Cassier Chauvat, Corinne" uniqKey="Cassier Chauvat C" first="Corinne" last="Cassier-Chauvat">Corinne Cassier-Chauvat</name><name sortKey="Chauvat, Franck" sort="Chauvat, Franck" uniqKey="Chauvat F" first="Franck" last="Chauvat">Franck Chauvat</name><name sortKey="Saguez, Cyril" sort="Saguez, Cyril" uniqKey="Saguez C" first="Cyril" last="Saguez">Cyril Saguez</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Picciocchi, Antoine" sort="Picciocchi, Antoine" uniqKey="Picciocchi A" first="Antoine" last="Picciocchi">Antoine Picciocchi</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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