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

Identifieur interne : 000529 ( Main/Exploration ); précédent : 000528; suivant : 000530

N-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 :

RBID : pubmed:26302480

Descripteurs français

English descriptors

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:


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Le document en format XML

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<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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