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J. Biol. Chem., Vol. 281, Issue 24, 16256-16263, June 16, 2006

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Iron-Sulfur Cluster Biosynthesis

CHARACTERIZATION OF ESCHERICHIA COLI CYaY AS AN IRON DONOR FOR THE ASSEMBLY OF [2Fe-2S] CLUSTERS IN THE SCAFFOLD IscU^*

Gunhild Layer¹, Sandrine Ollagnier-de Choudens², Yiannis Sanakis, and Marc Fontecave³

From the Laboratoire de Chimie et Biochimie des Centres Rédox Biologiques, DRDC/CB, Commissariat à l'Energie Atomique/CNRS/Université Joseph Fourier, CEA-Grenoble, UMR 5047, 17 Avenue des Martyrs, 38054 Grenoble Cedex 09, France and the NCSR, Demokritos, Institute of Materials Science, 15310 Ag. Paraskevi, Attiki, Department of Biological Applications and Technologies, University of Ioannina, 45110 Ioannina, Greece

The biogenesis of iron-sulfur [Fe-S] clusters requires the coordinated delivery of both iron and sulfide. Sulfide is provided by cysteine desulfurases that use L-cysteine as sulfur source. So far, the physiological iron donor has not been clearly identified. CyaY, the bacterial ortholog of frataxin, an iron binding protein thought to be involved in iron-sulfur cluster formation in eukaryotes, is a good candidate because it was shown to bind iron. Nevertheless, no functional in vitro studies showing an involvement of CyaY in [Fe-S] cluster biosynthesis have been reported so far. In this paper we demonstrate for the first time a specific interaction between CyaY and IscS, a cysteine desulfurase participating in iron-sulfur cluster assembly. Analysis of the iron-loaded CyaY protein demonstrated a strong binding of Fe³⁺ and a weak binding of Fe²⁺ by CyaY. Biochemical analysis showed that the CyaY-Fe³⁺ protein corresponds to a mixture of monomer, intermediate forms (dimer-pentamers), and oligomers with the intermediate one corresponding to the only stable and soluble iron-containing form of CyaY. Using spectroscopic methods, this form was further demonstrated to be functional in vitro as an iron donor during [Fe-S] cluster assembly on the scaffold protein IscU in the presence of IscS and cysteine. All of these results point toward a link between CyaY and [Fe-S] cluster biosynthesis, and a possible mechanism for the process is discussed.

Received for publication, December 21, 2005 , and in revised form, April 7, 2006.

^* This work was supported by the Greek Ministry of Development and General Secretariat for Research and Technology. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by a post-doctoral fellowship grant from the European Molecular Biology Organization.

² To whom correspondence may be addressed: Laboratoire de Chimie et Biochimie des Centres Rédox Biologiques, DRDC/CB, CEA/CNRS/Université Joseph Fourier, CEA-Grenoble, UMR 5047, 17 Ave. des Martyrs, 38054 Grenoble Cedex 09, France. Tel.: 33-4-38-78-91-15; Fax: 33-4-38-78-91-24; E-mail: sollagnier{at}cea.fr. ³ To whom correspondence may be addressed: Laboratoire de Chimie et Biochimie des Centres Rédox Biologiques, DRDC/CB, CEA/CNRS/Université Joseph Fourier, CEA-Grenoble, UMR 5047, 17 Ave. des Martyrs, 38054 Grenoble Cedex 09, France. Tel.: 33-4-38-78-91-03; Fax: 33-4-38-78-91-24; E-mail: mfontecave{at}cea.fr.

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