N-terminal domains mediate [2Fe-2S] cluster transfer from glutaredoxin-3 to anamorsin.
Identifieur interne : 000529 ( Main/Exploration ); précédent : 000528; suivant : 000530N-terminal domains mediate [2Fe-2S] cluster transfer from glutaredoxin-3 to anamorsin.
Auteurs : Lucia Banci [Italie] ; Simone Ciofi-Baffoni [Italie] ; Karolina Gajda [Italie] ; Riccardo Muzzioli [Italie] ; Riccardo Peruzzini [Italie] ; Julia Winkelmann [Italie]Source :
- Nature chemical biology [ 1552-4469 ] ; 2015.
Descripteurs français
- KwdFr :
- Apoprotéines (composition chimique), Apoprotéines (métabolisme), Cytosol (métabolisme), Escherichia coli (génétique), Fer (métabolisme), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (génétique), Ferrosulfoprotéines (métabolisme), Humains (MeSH), Liaison aux protéines (MeSH), Modèles biologiques (MeSH), Motifs et domaines d'intéraction protéique (MeSH), Protéines de transport (composition chimique), Protéines de transport (génétique), Protéines de transport (métabolisme), Protéines et peptides de signalisation intracellulaire (composition chimique), Protéines et peptides de signalisation intracellulaire (génétique), Protéines et peptides de signalisation intracellulaire (métabolisme), Simulation de docking moléculaire (MeSH), Transport des protéines (MeSH).
- MESH :
- composition chimique : Apoprotéines, Ferrosulfoprotéines, Protéines de transport, Protéines et peptides de signalisation intracellulaire.
- génétique : Escherichia coli, Ferrosulfoprotéines, Protéines de transport, Protéines et peptides de signalisation intracellulaire.
- métabolisme : Apoprotéines, Cytosol, Fer, Ferrosulfoprotéines, Protéines de transport, Protéines et peptides de signalisation intracellulaire.
- Humains, Liaison aux protéines, Modèles biologiques, Motifs et domaines d'intéraction protéique, Simulation de docking moléculaire, Transport des protéines.
English descriptors
- KwdEn :
- Apoproteins (chemistry), Apoproteins (metabolism), Carrier Proteins (chemistry), Carrier Proteins (genetics), Carrier Proteins (metabolism), Cytosol (metabolism), Escherichia coli (genetics), Humans (MeSH), Intracellular Signaling Peptides and Proteins (chemistry), Intracellular Signaling Peptides and Proteins (genetics), Intracellular Signaling Peptides and Proteins (metabolism), Iron (metabolism), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (metabolism), Models, Biological (MeSH), Molecular Docking Simulation (MeSH), Protein Binding (MeSH), Protein Interaction Domains and Motifs (MeSH), Protein Transport (MeSH).
- MESH :
- chemical , chemistry : Apoproteins, Carrier Proteins, Intracellular Signaling Peptides and Proteins, Iron-Sulfur Proteins.
- chemical , genetics : Carrier Proteins, Intracellular Signaling Peptides and Proteins, Iron-Sulfur Proteins.
- chemical , metabolism : Apoproteins, Carrier Proteins, Intracellular Signaling Peptides and Proteins, Iron, Iron-Sulfur Proteins.
- genetics : Escherichia coli.
- metabolism : Cytosol.
- Humans, Models, Biological, Molecular Docking Simulation, Protein Binding, Protein Interaction Domains and Motifs, Protein Transport.
Abstract
In eukaryotes, cytosolic monothiol glutaredoxins are proteins implicated in intracellular iron trafficking and sensing via their bound [2Fe-2S] clusters. We define a new role of human cytosolic monothiol glutaredoxin-3 (GRX3) in transferring its [2Fe-2S] clusters to human anamorsin, a physical and functional protein partner of GRX3 in the cytosol, whose [2Fe-2S] cluster-bound form is involved in the biogenesis of cytosolic and nuclear Fe-S proteins. Specific protein recognition between the N-terminal domains of the two proteins is the mandatory requisite to promote the [2Fe-2S] cluster transfer from GRX3 to anamorsin.
DOI: 10.1038/nchembio.1892
PubMed: 26302480
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<front><div type="abstract" xml:lang="en">In eukaryotes, cytosolic monothiol glutaredoxins are proteins implicated in intracellular iron trafficking and sensing via their bound [2Fe-2S] clusters. We define a new role of human cytosolic monothiol glutaredoxin-3 (GRX3) in transferring its [2Fe-2S] clusters to human anamorsin, a physical and functional protein partner of GRX3 in the cytosol, whose [2Fe-2S] cluster-bound form is involved in the biogenesis of cytosolic and nuclear Fe-S proteins. Specific protein recognition between the N-terminal domains of the two proteins is the mandatory requisite to promote the [2Fe-2S] cluster transfer from GRX3 to anamorsin. </div>
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<Abstract><AbstractText>In eukaryotes, cytosolic monothiol glutaredoxins are proteins implicated in intracellular iron trafficking and sensing via their bound [2Fe-2S] clusters. We define a new role of human cytosolic monothiol glutaredoxin-3 (GRX3) in transferring its [2Fe-2S] clusters to human anamorsin, a physical and functional protein partner of GRX3 in the cytosol, whose [2Fe-2S] cluster-bound form is involved in the biogenesis of cytosolic and nuclear Fe-S proteins. Specific protein recognition between the N-terminal domains of the two proteins is the mandatory requisite to promote the [2Fe-2S] cluster transfer from GRX3 to anamorsin. </AbstractText>
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