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Analyse fonctionnelle de protéines métal- ou redox- dépendantes chez les plantes

Abstract : The presence of reactive cysteines confers redox properties and/or the ability to bind metal ions to numerous proteins. This project, organized in several axes, aimed at characterizing proteins with a conserved CxxC motif and possibly a thioredoxin (TRX) fold in plants. It appears that the mitochondrial TRX o1 and o2, the atypical protein disulfide isomerase PDI-A and the chloroplastic glutaredoxin (GRX) S16 from A. thaliana expressed as recombinant proteins in Escherichia coli all incorporated an Fe-S center within homodimers whose function remains to be determined. Analysis of the redox properties of apo-proteins indicates that PDI-A and GRXS16 have little or no oxidoreductase activity respectively although intramolecular disulfide bridges are formed between conserved cysteines. In the case of GRXS16, its redox state would be regulated by light as the disulfide bridge is reducible by TRX but not by glutathione. The last research axis concerned the study of the properties of the MIA40 oxidoreductase and the ERV1 flavine oxidase, involved in the import and oxidative folding of proteins within the inter-membrane space of mitochondria. The results suggest that the singularity of this system in plants is based on the atypical structure of ERV1 and its ability to oxidize proteins in the presence of glutathione but in the absence of MIA40, which is essential in yeast or humans.
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Submitted on : Thursday, September 3, 2020 - 3:13:43 PM
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Flavien Zannini. Analyse fonctionnelle de protéines métal- ou redox- dépendantes chez les plantes. Biologie végétale. Université de Lorraine, 2019. Français. ⟨NNT : 2019LORR0276⟩. ⟨tel-02558987⟩



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