Structural bases for the interaction of frataxin with the central components of iron–sulphur cluster assembly

Filippo Prischi, Petr V. Konarev, Clara Iannuzzi, Chiara Pastore, Salvatore Adinolfi, Stephen R. Martin, Dmitri I. Svergun and Annalisa Pastore ()
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Filippo Prischi: National Institute for Medical Research, The Ridgeway
Petr V. Konarev: European Molecular Biology Laboratory, EMBL c/o DESY
Clara Iannuzzi: National Institute for Medical Research, The Ridgeway
Chiara Pastore: National Institute for Medical Research, The Ridgeway
Salvatore Adinolfi: National Institute for Medical Research, The Ridgeway
Stephen R. Martin: National Institute for Medical Research, The Ridgeway
Dmitri I. Svergun: European Molecular Biology Laboratory, EMBL c/o DESY
Annalisa Pastore: National Institute for Medical Research, The Ridgeway

Nature Communications, 2010, vol. 1, issue 1, 1-10

Abstract: Abstract Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich's ataxia. Independent reports have linked frataxin to iron–sulphur cluster assembly through interactions with the two central components of this machinery: desulphurase Nfs1/IscS and the scaffold protein Isu/IscU. In this study, we use a combination of biophysical methods to define the structural bases of the interaction of CyaY (the bacterial orthologue of frataxin) with the IscS/IscU complex. We show that CyaY binds IscS as a monomer in a pocket between the active site and the IscS dimer interface. Recognition does not require iron and occurs through electrostatic interactions of complementary charged residues. Mutations at the complex interface affect the rates of enzymatic cluster formation. CyaY binding strengthens the affinity of the IscS/IscU complex. Our data suggest a new paradigm for understanding the role of frataxin as a regulator of IscS functions.

Date: 2010
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DOI: 10.1038/ncomms1097

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