Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1.
Identifieur interne : 003B72 ( Main/Corpus ); précédent : 003B71; suivant : 003B73Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1.
Auteurs : Nicolas Rouhier ; 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.
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
Links to Exploration step
pubmed:17460036Le document en format XML
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<term>Disulfides (metabolism)</term>
<term>Escherichia coli (genetics)</term>
<term>Escherichia coli (metabolism)</term>
<term>Gene Expression (MeSH)</term>
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<term>Glutathione (chemistry)</term>
<term>Glutathione (metabolism)</term>
<term>Iron (metabolism)</term>
<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
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<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>
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<term>Iron-Sulfur Proteins</term>
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<term>Mutagenesis, Site-Directed</term>
<term>Protein Binding</term>
<term>Protein Structure, Quaternary</term>
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<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>
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<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>
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