GlutaredoxinV1, Main, Exploration, bibRecord, 000854

Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2.

Identifieur interne : 000854 ( Main/Exploration ); précédent : 000853; suivant : 000855

Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2.

Auteurs : Haoran Li [États-Unis] ; Daphne T. Mapolelo ; Sajini Randeniya ; Michael K. Johnson ; Caryn E. Outten

Source :

Biochemistry [ 1520-4995 ] ; 2012.

RBID : pubmed:22309771

Descripteurs français

KwdFr :
- Dichroïsme circulaire (MeSH), Dimérisation (MeSH), Données de séquences moléculaires (MeSH), Fer (métabolisme), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (métabolisme), Humains (MeSH), Protéines de transport (composition chimique), Protéines de transport (métabolisme), Sites de fixation (MeSH), Spectroscopie de résonance de spin électronique (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH).
MESH :
- composition chimique : Ferrosulfoprotéines, Protéines de transport.
- métabolisme : Fer, Ferrosulfoprotéines, Protéines de transport.
- Dichroïsme circulaire, Dimérisation, Données de séquences moléculaires, Humains, Sites de fixation, Spectroscopie de résonance de spin électronique, Structure tertiaire des protéines, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Carrier Proteins (chemistry), Carrier Proteins (metabolism), Circular Dichroism (MeSH), Dimerization (MeSH), Electron Spin Resonance Spectroscopy (MeSH), Humans (MeSH), Iron (metabolism), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Molecular Sequence Data (MeSH), Protein Structure, Tertiary (MeSH).
MESH :
- chemical , chemistry : Carrier Proteins, Iron-Sulfur Proteins.
- chemical , metabolism : Carrier Proteins, Iron, Iron-Sulfur Proteins.
- Amino Acid Sequence, Binding Sites, Circular Dichroism, Dimerization, Electron Spin Resonance Spectroscopy, Humans, Molecular Sequence Data, Protein Structure, Tertiary.

Abstract

Human glutaredoxin 3 (Glrx3) is an essential [2Fe-2S]-binding protein with ill-defined roles in immune cell response, embryogenesis, cancer cell growth, and regulation of cardiac hypertrophy. Similar to other members of the CGFS monothiol glutaredoxin (Grx) family, human Glrx3 forms homodimers bridged by two [2Fe-2S] clusters that are ligated by the conserved CGFS motifs and glutathione (GSH). We recently demonstrated that the yeast homologues of human Glrx3 and the yeast BolA-like protein Fra2 form [2Fe-2S]-bridged heterodimers that play a key role in signaling intracellular iron availability. Herein, we provide biophysical and biochemical evidence that the two tandem Grx-like domains in human Glrx3 form similar [2Fe-2S]-bridged complexes with human BolA2. UV-visible absorption and circular dichroism, resonance Raman, and electron paramagnetic resonance spectroscopic analyses of recombinant [2Fe-2S] Glrx3 homodimers and [2Fe-2S] Glrx3-BolA2 complexes indicate that the Fe-S coordination environments in these complexes are virtually identical to those of the analogous complexes in yeast. Furthermore, we demonstrate that apo BolA2 binds to each Grx domain in the [2Fe-2S] Glrx3 homodimer forming a [2Fe-2S] BolA2-Glrx3 heterotrimer. Taken together, these results suggest that the unusual [2Fe-2S]-bridging Grx-BolA interaction is conserved in higher eukaryotes and may play a role in signaling cellular iron status in humans.

DOI: 10.1021/bi2019089
PubMed: 22309771
PubMed Central: PMC3331715

Affiliations:

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

to stream Main, to step Corpus: 000866
to stream Main, to step Curation: 000866

Le document en format XML

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<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Protéines de transport (composition chimique)</term>
<term>Protéines de transport (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
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<term>Sites de fixation</term>
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<front><div type="abstract" xml:lang="en">Human glutaredoxin 3 (Glrx3) is an essential [2Fe-2S]-binding protein with ill-defined roles in immune cell response, embryogenesis, cancer cell growth, and regulation of cardiac hypertrophy. Similar to other members of the CGFS monothiol glutaredoxin (Grx) family, human Glrx3 forms homodimers bridged by two [2Fe-2S] clusters that are ligated by the conserved CGFS motifs and glutathione (GSH). We recently demonstrated that the yeast homologues of human Glrx3 and the yeast BolA-like protein Fra2 form [2Fe-2S]-bridged heterodimers that play a key role in signaling intracellular iron availability. Herein, we provide biophysical and biochemical evidence that the two tandem Grx-like domains in human Glrx3 form similar [2Fe-2S]-bridged complexes with human BolA2. UV-visible absorption and circular dichroism, resonance Raman, and electron paramagnetic resonance spectroscopic analyses of recombinant [2Fe-2S] Glrx3 homodimers and [2Fe-2S] Glrx3-BolA2 complexes indicate that the Fe-S coordination environments in these complexes are virtually identical to those of the analogous complexes in yeast. Furthermore, we demonstrate that apo BolA2 binds to each Grx domain in the [2Fe-2S] Glrx3 homodimer forming a [2Fe-2S] BolA2-Glrx3 heterotrimer. Taken together, these results suggest that the unusual [2Fe-2S]-bridging Grx-BolA interaction is conserved in higher eukaryotes and may play a role in signaling cellular iron status in humans.</div>
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<Abstract><AbstractText>Human glutaredoxin 3 (Glrx3) is an essential [2Fe-2S]-binding protein with ill-defined roles in immune cell response, embryogenesis, cancer cell growth, and regulation of cardiac hypertrophy. Similar to other members of the CGFS monothiol glutaredoxin (Grx) family, human Glrx3 forms homodimers bridged by two [2Fe-2S] clusters that are ligated by the conserved CGFS motifs and glutathione (GSH). We recently demonstrated that the yeast homologues of human Glrx3 and the yeast BolA-like protein Fra2 form [2Fe-2S]-bridged heterodimers that play a key role in signaling intracellular iron availability. Herein, we provide biophysical and biochemical evidence that the two tandem Grx-like domains in human Glrx3 form similar [2Fe-2S]-bridged complexes with human BolA2. UV-visible absorption and circular dichroism, resonance Raman, and electron paramagnetic resonance spectroscopic analyses of recombinant [2Fe-2S] Glrx3 homodimers and [2Fe-2S] Glrx3-BolA2 complexes indicate that the Fe-S coordination environments in these complexes are virtually identical to those of the analogous complexes in yeast. Furthermore, we demonstrate that apo BolA2 binds to each Grx domain in the [2Fe-2S] Glrx3 homodimer forming a [2Fe-2S] BolA2-Glrx3 heterotrimer. Taken together, these results suggest that the unusual [2Fe-2S]-bridging Grx-BolA interaction is conserved in higher eukaryotes and may play a role in signaling cellular iron status in humans.</AbstractText>
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Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2.

Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2.

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