N-terminal domains mediate [2Fe-2S] cluster transfer from glutaredoxin-3 to anamorsin

• DOI: 10.1038/nchembio.1892
• Publication Date: 2015-08-24T16:43:39Z
• Authors: Lucia Banci; Simone Ciofi-Baffoni; Karolina Gajda; Riccardo Muzzioli; Riccardo Peruzzini; Julia Winkelmann
• Keywords: Iron-Sulfur Proteins; 0303 health sciences; Iron; Intracellular Signaling Peptides and Proteins; Models, Biological; Biochemistry; Molecular Biology;monothiol glutaredoxins; anamorsin:GLRX3; iron-sulfur protein biogenesis; Molecular Docking Simulation; Protein Transport; 03 medical and health sciences; Cytosol; Escherichia coli; Humans; Protein Interaction Domains and Motifs; Apoproteins; Carrier Proteins; Protein Binding

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.