2 results match your criteria: "Laboratoire de Biophysique Moléculaire et Cellulaire - UMR-CNRS 5090-Université Joseph-Fourier[Affiliation]"

Aconitases are iron-sulfur hydrolyases catalysing the interconversion of citrate and isocitrate in a wide variety of organisms. Eukaryotic aconitases have been assigned additional roles, as in the case of the metazoan dual activity cytosolic aconitase-iron regulatory protein 1 (IRP1). This human protein was produced in yeast mitochondria to probe IRP1 folding in this organelle where iron-sulfur synthesis originates.

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Zinc and cadmium specifically interfere with RNA-binding activity of human iron regulatory protein 1.

J Inorg Biochem

August 2004

Département Réponse et Dynamique Cellulaires, Laboratoire de Biophysique Moléculaire et Cellulaire - UMR-CNRS 5090-Université Joseph-Fourier, Commissariat à l'Energie Atomique de Grenoble, 17 avenue des Martyrs, 38054 Grenoble cedex 9, France.

The cellular pro-oxidative stress induced by high zinc concentrations or cadmium is most likely mediated by disruption of redox (mainly thiol) homeostasis or by mishandling of redox-active transition metals. The impact of zinc and cadmium on the main regulators of iron homeostasis in metazoans, the iron regulatory proteins (IRP) 1 and 2, has been probed with the human recombinant proteins. Using purified proteins or extracts of yeast producing human IRP, zinc and cadmium were shown to interfere with the IRE-binding activity of IRP1, but not with that of IRP2 or the aconitase activity of IRP1.

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