IBA57 Recruits ISCA2 to Form a [2Fe-2S] Cluster-Mediated Complex
| Autor: | Spyridon Gourdoupis, Vito Calderone, Veronica Nasta, Lucia Banci, Simone Ciofi-Baffoni |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
030102 biochemistry & molecular biology Protein family Chemistry IBA57 iron-sulphur cluster General Chemistry Oxidative phosphorylation Plasma protein binding Biochemistry Aconitase Catalysis In vitro Cell biology 03 medical and health sciences 030104 developmental biology Colloid and Surface Chemistry GLRX5 Cluster (physics) Cysteine |
| Zdroj: | Journal of the American Chemical Society 'Journal of the American Chemical Society ', vol: 140, pages: 14401-14412 (2018) |
| ISSN: | 0002-7863 |
| DOI: | 10.1021/jacs.8b09061 |
| Popis: | The maturation of mitochondrial iron-sulfur proteins requires a complex protein machinery. Human IBA57 protein was proposed to act in a late phase of this machinery, along with GLRX5, ISCA1, and ISCA2. However, a molecular picture on how these proteins cooperate is not defined yet. We show here that IBA57 forms a heterodimeric complex with ISCA2 by bridging a [2Fe-2S] cluster, that [2Fe-2S] cluster binding is absolutely required to promote the complex formation, and that the cysteine of the conserved motif characterizing IBA57 protein family and the three conserved cysteines of the ISCA protein family act as cluster ligands. The [2Fe-2S] heterodimeric complex is the final product when IBA57 is either exposed to [2Fe-2S] ISCA2 or in the presence of [2Fe-2S] GLRX5 and apo ISCA2. We also find that the [2Fe-2S] ISCA2-IBA57 complex is resistant to highly oxidative environments and is capable of reactivating apo aconitase in vitro. Collectively, our data delinate a [2Fe-2S] cluster transfer pathway involving three partner proteins of the mitochondrial ISC machinery, that is, GLRX5, ISCA2 and IBA57, which leads to the formation of a [2Fe-2S] ISCA2-IBA57 complex. |
| Databáze: | OpenAIRE |
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