GlutaredoxinV1, Main, Exploration, bibRecord, 000E26

Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor.

Identifieur interne : 000E26 ( Main/Exploration ); précédent : 000E25; suivant : 000E27

Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor.

Auteurs : Christopher Horst Lillig [Suède] ; Carsten Berndt ; Olivia Vergnolle ; Maria Elisabet Lönn ; Christoph Hudemann ; Eckhard Bill ; Arne Holmgren

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2005.

RBID : pubmed:15917333

Descripteurs français

English descriptors

KwdEn :
- Apoproteins (chemistry), Apoproteins (metabolism), Circular Dichroism (MeSH), Enzyme Activation (MeSH), Enzyme Stability (MeSH), Enzyme-Linked Immunosorbent Assay (MeSH), Glutaredoxins (MeSH), HeLa Cells (MeSH), Holoenzymes (chemistry), Holoenzymes (metabolism), Humans (MeSH), Immunoprecipitation (MeSH), Iron (metabolism), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Kinetics (MeSH), Models, Molecular (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Protein Binding (MeSH), Protein Structure, Secondary (MeSH), Structure-Activity Relationship (MeSH).
MESH :
- chemical , chemistry : Apoproteins, Holoenzymes, Iron-Sulfur Proteins, Oxidoreductases.
- chemical , metabolism : Apoproteins, Holoenzymes, Iron, Iron-Sulfur Proteins, Oxidoreductases.
- Circular Dichroism, Enzyme Activation, Enzyme Stability, Enzyme-Linked Immunosorbent Assay, Glutaredoxins, HeLa Cells, Humans, Immunoprecipitation, Kinetics, Models, Molecular, Oxidation-Reduction, Protein Binding, Protein Structure, Secondary, Structure-Activity Relationship.

Abstract

Human mitochondrial glutaredoxin 2 (Grx2) is a glutathione-dependent oxidoreductase (active site: Cys-Ser-Tyr-Cys) that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Here, we have characterized Grx2 as an iron-sulfur center-containing member of the thioredoxin fold protein family. Mossbauer spectroscopy revealed the presence of a four cysteine-coordinated nonoxidizable [2Fe-2S]2+ cluster that bridges two Grx2 molecules via two structural Cys residues to form dimeric holo Grx2. Coimmunoprecipitation of radiolabeled iron with Grx2 from human cell lines indicated the presence of the cluster in vivo. The [2Fe-2S]-bridged dimer was enzymatically inactive, but degradation of the cluster and the resulting monomerization of Grx2 activated the protein. Slow degradation under aerobic conditions was prevented by the presence of glutathione, whereas glutathione disulfide as well as one-electron oxidants or reductants promoted monomerization of Grx2. We propose that the iron-sulfur cluster serves as a redox sensor for the activation of Grx2 during conditions of oxidative stress when free radicals are formed and the glutathione pool becomes oxidized.

DOI: 10.1073/pnas.0500735102
PubMed: 15917333
PubMed Central: PMC1149418

Affiliations:

Suède

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000E07
to stream Main, to step Curation: 000E07

Le document en format XML

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<term>Enzyme Activation (MeSH)</term>
<term>Enzyme Stability (MeSH)</term>
<term>Enzyme-Linked Immunosorbent Assay (MeSH)</term>
<term>Glutaredoxins (MeSH)</term>
<term>HeLa Cells (MeSH)</term>
<term>Holoenzymes (chemistry)</term>
<term>Holoenzymes (metabolism)</term>
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<term>Immunoprecipitation (MeSH)</term>
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<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
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<term>Oxidoreductases (metabolism)</term>
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<term>Apoprotéines (métabolisme)</term>
<term>Cellules HeLa (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Dichroïsme circulaire (MeSH)</term>
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<term>Ferrosulfoprotéines (métabolisme)</term>
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<term>Holoenzymes (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Immunoprécipitation (MeSH)</term>
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<term>Oxidoreductases (métabolisme)</term>
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<term>Relation structure-activité (MeSH)</term>
<term>Stabilité enzymatique (MeSH)</term>
<term>Structure secondaire des protéines (MeSH)</term>
<term>Test ELISA (MeSH)</term>
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<front><div type="abstract" xml:lang="en">Human mitochondrial glutaredoxin 2 (Grx2) is a glutathione-dependent oxidoreductase (active site: Cys-Ser-Tyr-Cys) that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Here, we have characterized Grx2 as an iron-sulfur center-containing member of the thioredoxin fold protein family. Mossbauer spectroscopy revealed the presence of a four cysteine-coordinated nonoxidizable [2Fe-2S]2+ cluster that bridges two Grx2 molecules via two structural Cys residues to form dimeric holo Grx2. Coimmunoprecipitation of radiolabeled iron with Grx2 from human cell lines indicated the presence of the cluster in vivo. The [2Fe-2S]-bridged dimer was enzymatically inactive, but degradation of the cluster and the resulting monomerization of Grx2 activated the protein. Slow degradation under aerobic conditions was prevented by the presence of glutathione, whereas glutathione disulfide as well as one-electron oxidants or reductants promoted monomerization of Grx2. We propose that the iron-sulfur cluster serves as a redox sensor for the activation of Grx2 during conditions of oxidative stress when free radicals are formed and the glutathione pool becomes oxidized.</div>
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<Abstract><AbstractText>Human mitochondrial glutaredoxin 2 (Grx2) is a glutathione-dependent oxidoreductase (active site: Cys-Ser-Tyr-Cys) that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Here, we have characterized Grx2 as an iron-sulfur center-containing member of the thioredoxin fold protein family. Mossbauer spectroscopy revealed the presence of a four cysteine-coordinated nonoxidizable [2Fe-2S]2+ cluster that bridges two Grx2 molecules via two structural Cys residues to form dimeric holo Grx2. Coimmunoprecipitation of radiolabeled iron with Grx2 from human cell lines indicated the presence of the cluster in vivo. The [2Fe-2S]-bridged dimer was enzymatically inactive, but degradation of the cluster and the resulting monomerization of Grx2 activated the protein. Slow degradation under aerobic conditions was prevented by the presence of glutathione, whereas glutathione disulfide as well as one-electron oxidants or reductants promoted monomerization of Grx2. We propose that the iron-sulfur cluster serves as a redox sensor for the activation of Grx2 during conditions of oxidative stress when free radicals are formed and the glutathione pool becomes oxidized.</AbstractText>
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<ReferenceList><Reference><Citation>Mol Cell Biol. 1999 Dec;19(12):8180-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10567543</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2005 Feb 18;327(3):774-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15649413</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Inorg Chem. 2000 Feb;5(1):2-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10766431</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2000 Jul 14;300(3):587-95</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10884354</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2000 Jul 21;274(1):177-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10903915</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Biochem Sci. 2000 Aug;25(8):352-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10916152</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2000 Aug 25;275(34):26556-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10854441</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2000 Aug 15;1459(2-3):370-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11004453</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2000 Winter;2(4):811-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11213485</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2001 Jan 12;276(2):1335-44</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11035035</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2001 Jul 13;276(28):26269-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11297543</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2001 Aug 10;276(32):30374-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11397793</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 2002;347:286-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11898418</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Biol Cell. 2002 Apr;13(4):1109-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11950925</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 2002 Jun 15;364(Pt 3):617-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11958675</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2003 May 30;278(22):19603-10</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12649289</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Am Chem Soc. 2003 May 21;125(20):6078-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12785837</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2003 Jul 11;278(28):25745-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12730244</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2003 Sep 15;22(18):4815-25</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12970193</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2004 Feb 20;303(5661):1185-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14976313</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 Feb 27;279(9):7537-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14676218</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2004 Jul 2;319(3):801-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15184054</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13227-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15328416</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1976 Jul;73(7):2275-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7783</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1979 May 10;254(9):3672-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">34620</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1982 Jun 25;257(12):6686-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7045093</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1988;158:357-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3374387</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1989 Aug 25;264(24):13963-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2668278</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1990 Sep 15;265(26):15361-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2394726</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1992 Sep 29;31(38):9288-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1390715</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1995;252:283-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7476363</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1997 Apr 25;272(17):11236-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9111025</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):6635-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9192617</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1997 Aug 1;277(5326):653-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9235882</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1998 Jan 2;273(1):392-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9417094</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1998 May 19;37(20):7070-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9585516</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1999 Mar 19;274(12):7695-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10075658</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Chem Biol. 1999 Apr;3(2):152-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10226040</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Immunol Lett. 1999 Jun 1;68(2-3):397-401</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10424449</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Free Radic Res. 1999 Oct;31(4):357-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10517541</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1956 Jan;218(1):97-106</Citation>
<ArticleIdList><ArticleId IdType="pubmed">13278318</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 Nov 12;279(46):47939-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15347644</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 Dec 10;279(50):51923-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15456753</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2000 Mar 16;269(2):451-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10708574</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor.

Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor.

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