Caractérisation structurale d'états oligomériques de protéines impliquées dans l'homéostasie du fer : les protéines BolA et les glutarédoxines

Abstract : Intermolecular interactions in living cells are complex and help convey the information indispensable to the survival of the organism at a given time. It even happens that various stakeholders are involved at different stages of the same process. Among many biological processes present within living cells, the biogenesis of iron-sulfur clusters appears to be very complex. This complexity is probably related to cellular toxicity of both free iron and free sulfur. Thus the different stages of iron-sulfur clusters biosynthesis must be tightly regulated. Recent studies highlight that BolA proteins and class II glutaredoxins are involved in iron homeostasis probably by acting alone or in a concerted manner. However, the current function of these proteins in the various steps of the iron-sulfur clusters biogenesis is yet unidentified. To better understand how BolA proteins and glutaredoxins fulfill their biological function, we studied throughout this PhD work the ability of Arabidopsis thaliana proteins to form homodimers and heterodimers. To do this, X-ray crystallography, nuclear magnetic resonance and other spectroscopic methods were used to structurally characterize the different oligomeric states of these two proteins
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Thomas Roret. Caractérisation structurale d'états oligomériques de protéines impliquées dans l'homéostasie du fer : les protéines BolA et les glutarédoxines. Autre [cond-mat.other]. Université de Lorraine, 2014. Français. ⟨NNT : 2014LORR0250⟩. ⟨tel-01751272⟩

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