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The structure of E. coli IscX consists of a classical helix-turn-helix fold often found in transcription regulators (Shimomura et al., 2005; Pastore et al., 2006). In vitro studies have shown that IscX is able to bind IscS, thus suggesting a role for IscX as a molecular adaptor (Pastore et al., 2006; Shi et al., 2010; Kim et al., 2014). IscX also binds to iron, although with an affinity at least one order of magnitude weaker than that of CyaY, through a negatively charged surface, the same by which it recognizes IscS (Pastore et al., 2006). An exposed negatively charged iron binding surface which overlaps with the surface of interaction with IscS is also a feature present in another protein, CyaY (the ortholog in bacteria of the eukaryotic frataxin). This protein has attracted much attention because in humans it is associated with Friedreich's ataxia (Pastore and Puccio, 2013). In contrast to IscX, frataxins are proteins highly conserved from bacteria to high eukaryotes (Gibson et al., 1996) and are essential in eukaryotes (Li et al., 1999). In prokaryotes, CyaY is external to the isc operon but has extensively been implicated in Fe-S cluster assembly (Huynen et al., 2001). We have in the past shown that CyaY is an IscS regulator, which dictates the enzymatic assembly of Fe-S clusters (Adinolfi et al., 2009; Prischi et al., 2010a). Intriguingly, IscX and CyaY compete for the same site on IscS (Prischi et al., 2010a; Shi et al., 2010; Kim et al., 2014). A genetic interaction between CyaY and IscX was also demonstrated by a recent study which has validated a role of IscX as a new bona fide Fe-S cluster biogenesis factor (Roche et al., 2015). In some species, CyaY and IscX seem to replace each other. 153554b96e
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