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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Apoproteins / chemistry
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Apoproteins / metabolism
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Cytosol / metabolism
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Escherichia coli / genetics
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Humans
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Intracellular Signaling Peptides and Proteins / chemistry
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Intracellular Signaling Peptides and Proteins / genetics
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Intracellular Signaling Peptides and Proteins / metabolism*
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Iron / metabolism*
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Iron-Sulfur Proteins / chemistry
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Iron-Sulfur Proteins / genetics
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Iron-Sulfur Proteins / metabolism*
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Models, Biological
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Molecular Docking Simulation
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Protein Binding
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Protein Interaction Domains and Motifs
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Protein Transport
Substances
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Apoproteins
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CIAPIN1 protein, human
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Carrier Proteins
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GLRX3 protein, human
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Intracellular Signaling Peptides and Proteins
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Iron-Sulfur Proteins
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Iron