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M110938200v1
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Papers In Press, published online ahead of print January 25, 2002
J. Biol. Chem, 10.1074/jbc.M110938200
Submitted on November 15, 2001
Revised on January 9, 2002
Accepted on January 25, 2002

Structural changes associated with switching activities of the human iron regulatory protein 1

Xavier Brazzolotto, Peter Timmins, Yves Dupont, and Jean-Marc Moulis

Department of Biologie Moleculaire et Structurale, CEA-Grenoble, DBMS, 38054, Grenoble Cedex 9

Corresponding Author: jean-marc.moulis{at}cea.fr

Metazoan Iron Regulatory Protein 1 is a dual activity protein, being either an aconitase or a regulatory factor binding to messenger RNA involved in iron homeostasis. Sequence comparisons and site-directed mutagenesis experiments have supported a structural relationship between mitochondrial aconitase and Iron Regulatory Protein 1. The structural properties of human recombinant Iron Regulatory Protein 1 have been probed in the present work. Whereas iron-free Iron Regulatory Protein 1 displays a significantly larger radius of gyration measured by small-angle neutron scattering than calculated for mitochondrial aconitase, binding of either the [4Fe-4S] cluster needed for aconitase activity or of a RNA substrate turns Iron Regulatory Protein 1 into a more compact molecule. These conformational changes are associated with the gain of secondary structural elements as indicated by circular dichroism studies. They likely involve alpha-helices covering the substrate binding cleft of cytosolic aconitase, and they suggest an induced fit mechanism of Iron Responsive Element recognition. These studies refine previously proposed models of the 'iron-sulfur switch' driving the biological function of human Iron Regulatory Protein 1 and they provide a structural framework to probe the relevance of the numerous cellular molecules proposed to affect its function.


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