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Iron–sulphur (Fe-S) clusters are ubiquitous co-factors which require multi-protein systems for their synthesis. In  Mycobacterium tuberculosis , the  Rv1460-Rv1461-Rv1462-Rv1463-csd-Rv1465-Rv1466  operon ( suf  operon) encodes the primary Fe-S cluster biogenesis system. The first gene in this operon,  Rv1460 , shares homology with the cyanobacterial SufR, which functions as a transcriptional repressor of the  sufBCDS  operon. Rv1460’s function in  M .  tuberculosis  has however not been determined. In this study, we demonstrate that  M .  tuberculosis  mutants lacking a functional Rv1460 protein are impaired for growth under standard culture conditions. Elevated expression of  Rv1460  and  Rv1461  was observed in the mutant, implicating Rv1460 in the regulation of the  suf  operon. Binding of an Fe-S cluster to purified recombinant Rv1460 was confirmed by UV-visible spectroscopy and circular dichroism. Furthermore, three conserved cysteine residues, C203, C216 and C244, proposed to provide ligands for the coordination of an Fe-S cluster, were shown to be required for the function of Rv1460 in  M .  tuberculosis . Rv1460 therefore seems to be functionally analogous to cyanobacterial SufR.

Rv1460, a SufR homologue, is a repressor of the suf operon in Mycobacterium tuberculosis