Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1.
Identifieur interne : 003B85 ( Main/Exploration ); précédent : 003B84; suivant : 003B86Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1.
Auteurs : Nicolas Rouhier [France] ; Hideaki Unno ; Sibali Bandyopadhyay ; Lluis Masip ; Sung-Kun Kim ; Masakazu Hirasawa ; José Manuel Gualberto ; Virginie Lattard ; Masami Kusunoki ; David B. Knaff ; George Georgiou ; Toshiharu Hase ; Michael K. Johnson ; Jean-Pierre JacquotSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2007.
Descripteurs français
- KwdFr :
- Analyse spectrale (MeSH), Clonage moléculaire (MeSH), Cristallographie aux rayons X (MeSH), Disulfures (métabolisme), Escherichia coli (génétique), Escherichia coli (métabolisme), Expression des gènes (MeSH), Fer (métabolisme), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (métabolisme), Glutarédoxines (MeSH), Glutathion (composition chimique), Glutathion (métabolisme), Liaison aux protéines (MeSH), Ligands (MeSH), Lignée cellulaire (MeSH), Modèles moléculaires (MeSH), Mutagenèse dirigée (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Populus (métabolisme), Soufre (métabolisme), Structure quaternaire des protéines (MeSH), Structure tertiaire des protéines (MeSH), Tabac (MeSH).
- MESH :
- composition chimique : Ferrosulfoprotéines, Glutathion, Oxidoreductases.
- génétique : Escherichia coli, Oxidoreductases.
- métabolisme : Disulfures, Escherichia coli, Fer, Ferrosulfoprotéines, Glutathion, Oxidoreductases, Populus, Soufre.
- Analyse spectrale, Clonage moléculaire, Cristallographie aux rayons X, Expression des gènes, Glutarédoxines, Liaison aux protéines, Ligands, Lignée cellulaire, Modèles moléculaires, Mutagenèse dirigée, Structure quaternaire des protéines, Structure tertiaire des protéines, Tabac.
English descriptors
- KwdEn :
- Cell Line (MeSH), Cloning, Molecular (MeSH), Crystallography, X-Ray (MeSH), Disulfides (metabolism), Escherichia coli (genetics), Escherichia coli (metabolism), Gene Expression (MeSH), Glutaredoxins (MeSH), Glutathione (chemistry), Glutathione (metabolism), Iron (metabolism), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Ligands (MeSH), Models, Molecular (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidoreductases (chemistry), Oxidoreductases (genetics), Oxidoreductases (metabolism), Populus (metabolism), Protein Binding (MeSH), Protein Structure, Quaternary (MeSH), Protein Structure, Tertiary (MeSH), Spectrum Analysis (MeSH), Sulfur (metabolism), Tobacco (MeSH).
- MESH :
- chemical , chemistry : Glutathione, Iron-Sulfur Proteins, Oxidoreductases.
- chemical , genetics : Oxidoreductases.
- chemical , metabolism : Disulfides, Glutathione, Iron, Iron-Sulfur Proteins, Oxidoreductases, Sulfur.
- genetics : Escherichia coli.
- metabolism : Escherichia coli, Populus.
- Cell Line, Cloning, Molecular, Crystallography, X-Ray, Gene Expression, Glutaredoxins, Ligands, Models, Molecular, Mutagenesis, Site-Directed, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary, Spectrum Analysis, Tobacco.
Abstract
When expressed in Escherichia coli, cytosolic poplar glutaredoxin C1 (CGYC active site) exists as a dimeric iron-sulfur-containing holoprotein or as a monomeric apoprotein in solution. Analytical and spectroscopic studies of wild-type protein and site-directed variants and structural characterization of the holoprotein by using x-ray crystallography indicate that the holoprotein contains a subunit-bridging [2Fe-2S] cluster that is ligated by the catalytic cysteines of two glutaredoxins and the cysteines of two glutathiones. Mutagenesis data on a variety of poplar glutaredoxins suggest that the incorporation of an iron-sulfur cluster could be a general feature of plant glutaredoxins possessing a glycine adjacent to the catalytic cysteine. In light of these results, the possible involvement of plant glutaredoxins in oxidative stress sensing or iron-sulfur biosynthesis is discussed with respect to their intracellular localization.
DOI: 10.1073/pnas.0702268104
PubMed: 17460036
PubMed Central: PMC1863468
Affiliations:
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Johnson</name></author><author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Line (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Disulfides (metabolism)</term><term>Escherichia coli (genetics)</term><term>Escherichia coli (metabolism)</term><term>Gene Expression (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (chemistry)</term><term>Glutathione (metabolism)</term><term>Iron (metabolism)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Ligands (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Oxidoreductases (chemistry)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term><term>Populus (metabolism)</term><term>Protein Binding (MeSH)</term><term>Protein Structure, Quaternary (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Spectrum Analysis (MeSH)</term><term>Sulfur (metabolism)</term><term>Tobacco (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse spectrale (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Disulfures (métabolisme)</term><term>Escherichia coli (génétique)</term><term>Escherichia coli (métabolisme)</term><term>Expression des gènes (MeSH)</term><term>Fer (métabolisme)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (composition chimique)</term><term>Glutathion (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Ligands (MeSH)</term><term>Lignée cellulaire (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Oxidoreductases (composition chimique)</term><term>Oxidoreductases (génétique)</term><term>Oxidoreductases (métabolisme)</term><term>Populus (métabolisme)</term><term>Soufre (métabolisme)</term><term>Structure quaternaire des protéines (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Tabac (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutathione</term><term>Iron-Sulfur Proteins</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disulfides</term><term>Glutathione</term><term>Iron</term><term>Iron-Sulfur Proteins</term><term>Oxidoreductases</term><term>Sulfur</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Ferrosulfoprotéines</term><term>Glutathion</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfures</term><term>Escherichia coli</term><term>Fer</term><term>Ferrosulfoprotéines</term><term>Glutathion</term><term>Oxidoreductases</term><term>Populus</term><term>Soufre</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Cloning, Molecular</term><term>Crystallography, X-Ray</term><term>Gene Expression</term><term>Glutaredoxins</term><term>Ligands</term><term>Models, Molecular</term><term>Mutagenesis, Site-Directed</term><term>Protein Binding</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Tertiary</term><term>Spectrum Analysis</term><term>Tobacco</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse spectrale</term><term>Clonage moléculaire</term><term>Cristallographie aux rayons X</term><term>Expression des gènes</term><term>Glutarédoxines</term><term>Liaison aux protéines</term><term>Ligands</term><term>Lignée cellulaire</term><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term><term>Tabac</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">When expressed in Escherichia coli, cytosolic poplar glutaredoxin C1 (CGYC active site) exists as a dimeric iron-sulfur-containing holoprotein or as a monomeric apoprotein in solution. Analytical and spectroscopic studies of wild-type protein and site-directed variants and structural characterization of the holoprotein by using x-ray crystallography indicate that the holoprotein contains a subunit-bridging [2Fe-2S] cluster that is ligated by the catalytic cysteines of two glutaredoxins and the cysteines of two glutathiones. Mutagenesis data on a variety of poplar glutaredoxins suggest that the incorporation of an iron-sulfur cluster could be a general feature of plant glutaredoxins possessing a glycine adjacent to the catalytic cysteine. In light of these results, the possible involvement of plant glutaredoxins in oxidative stress sensing or iron-sulfur biosynthesis is discussed with respect to their intracellular localization.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17460036</PMID><DateCompleted><Year>2007</Year><Month>06</Month><Day>20</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0027-8424</ISSN><JournalIssue CitedMedium="Print"><Volume>104</Volume><Issue>18</Issue><PubDate><Year>2007</Year><Month>May</Month><Day>01</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1.</ArticleTitle><Pagination><MedlinePgn>7379-84</MedlinePgn></Pagination><Abstract><AbstractText>When expressed in Escherichia coli, cytosolic poplar glutaredoxin C1 (CGYC active site) exists as a dimeric iron-sulfur-containing holoprotein or as a monomeric apoprotein in solution. Analytical and spectroscopic studies of wild-type protein and site-directed variants and structural characterization of the holoprotein by using x-ray crystallography indicate that the holoprotein contains a subunit-bridging [2Fe-2S] cluster that is ligated by the catalytic cysteines of two glutaredoxins and the cysteines of two glutathiones. Mutagenesis data on a variety of poplar glutaredoxins suggest that the incorporation of an iron-sulfur cluster could be a general feature of plant glutaredoxins possessing a glycine adjacent to the catalytic cysteine. In light of these results, the possible involvement of plant glutaredoxins in oxidative stress sensing or iron-sulfur biosynthesis is discussed with respect to their intracellular localization.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Unité Mixte de Recherche 1136, Institut National de la Recherche Agronomique, Institut Fédératif de Recherche 110, Genomics, Ecology, Nancy University, BP 239, 54506 Vandoeuvre-lès-Nancy Cedex, France. nrouhier@scbiol.uhp-nancy.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Unno</LastName><ForeName>Hideaki</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Bandyopadhyay</LastName><ForeName>Sibali</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Masip</LastName><ForeName>Lluis</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Sung-Kun</ForeName><Initials>SK</Initials></Author><Author ValidYN="Y"><LastName>Hirasawa</LastName><ForeName>Masakazu</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Gualberto</LastName><ForeName>José Manuel</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Lattard</LastName><ForeName>Virginie</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Kusunoki</LastName><ForeName>Masami</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Knaff</LastName><ForeName>David B</ForeName><Initials>DB</Initials></Author><Author ValidYN="Y"><LastName>Georgiou</LastName><ForeName>George</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Hase</LastName><ForeName>Toshiharu</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Johnson</LastName><ForeName>Michael K</ForeName><Initials>MK</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>2E7P</AccessionNumber></AccessionNumberList></DataBank></DataBankList><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM062524</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R37 GM062524</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM62524</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>04</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</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>70FD1KFU70</RegistryNumber><NameOfSubstance UI="D013455">Sulfur</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName 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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="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein 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