The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX

Salvatore Adinolfi, Rita Puglisi, Jason C. Crack, Clara Iannuzzi, Fabrizio Dal Piaz, Petr V. Konarev, Dmitri I. Svergun, Stephen R. Martin, Nick E. Le Brun, Annalisa Pastore

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27 Citations (Scopus)

Abstract

scX (or YfhJ) is a protein of unknown function which takes part in the iron-sulfur cluster assembly machinery, a highly specialized and essential metabolic pathway. IscX binds to iron with low affinity and interacts with IscS, the desulfurase central to cluster assembly.
Previous studies have suggested a competition between IscX and CyaY, the bacterial
ortholog of frataxin, for the same binding surface of IscS. This competition could suggest
a link between the two proteins with a functional significance. Using a hybrid approach based on nuclear magnetic resonance, small angle scattering and biochemical methods,
we show here that IscX is a modulator of the inhibitory properties of CyaY: by competing for the same site on IscS, the presence of IscX rescues the rates of enzymatic cluster formation which are inhibited by CyaY. The effect is stronger at low iron concentrations, whereas it becomes negligible at high iron concentrations. These results strongly suggest
the mechanism of the dual regulation of iron sulfur cluster assembly under the control of
iron as the effector.
Original languageEnglish
JournalFrontiers in Molecular Biosciences
DOIs
Publication statusPublished - 2 Feb 2018

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