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.

N-terminal domains mediate [2Fe-2S] cluster transfer from glutaredoxin-3 to anamorsin / Banci, Lucia; Ciofi-Baffoni, Simone; Gajda, Karolina; Muzzioli, Riccardo; Peruzzini, Riccardo; Winkelmann, Julia. - In: NATURE CHEMICAL BIOLOGY. - ISSN 1552-4450. - STAMPA. - 11:(2015), pp. 772-778. [10.1038/nchembio.1892]

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

BANCI, LUCIA
;
CIOFI BAFFONI, SIMONE
;
GAJDA, KAROLINA;MUZZIOLI, RICCARDO;PERUZZINI, RICCARDO;WINKELMANN, JULIA
2015

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.
2015
11
772
778
Banci, Lucia; Ciofi-Baffoni, Simone; Gajda, Karolina; Muzzioli, Riccardo; Peruzzini, Riccardo; Winkelmann, Julia
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1013721
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