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Labile [4Fe-4S]2+ clusters found at the active sites of many dehydratases are susceptible to damage by univalent oxidants that convert the clusters to an inactive [3Fe-4S]1+ form. Bacteria repair damaged clusters in a process that does not requirede novo protein synthesis or the Isc and Suf cluster assembly pathways. The current study investigates the participation of the bacterial frataxin ortholog CyaY and the YggX protein, which are proposed to play roles in iron trafficking and iron-sulfur cluster repair. Previous reports found that individual mutations incyaY oryggX were not associated with phenotypic changes inEscherichia coli andSalmonella enterica serovar Typhimurium, suggesting that CyaY and YggX might have functionally redundant roles. However, we have found that individual mutations incyaY oryggX confer enhanced susceptibility to hydrogen peroxide inSalmonella enterica serovar Typhimurium. In addition, inactivation of thestm3944 open reading frame, which is located immediately upstream ofcyaY and which encodes a putative inner membrane protein, dramatically enhances the hydrogen peroxide sensitivity of acyaY mutant. Overexpression of STM3944 reduces the elevated intracellular free iron levels observed in anS . Typhimuriumfur mutant and also reduces the total cellular iron content under conditions of iron overload, suggesting that thestm3944 -encoded protein may mediate iron efflux. Mutations incyaY andyggX have different effects on the activities of the iron-sulfur cluster-containing aconitase, serine deaminase, and NADH dehydrogenase I enzymes ofS . Typhimurium under basal conditions or following recovery from oxidative stress. In addition,cyaY andyggX mutations have additive effects on 6-phosphogluconate dehydratase-dependent growth during nitrosative stress, and acyaY mutation reducesSalmonella virulence in mice. Collectively, these results indicate that CyaY and YggX play distinct supporting roles in iron-sulfur cluster biosynthesis and the repair of labile clusters damaged by univalent oxidants.Salmonella experiences oxidative and nitrosative stress within host phagocytes, and CyaY-dependent maintenance of labile iron-sulfur clusters appears to be important forSalmonella virulence.

Distinct Roles of the Salmonella enterica Serovar Typhimurium CyaY and YggX Proteins in the Biosynthesis and Repair of Iron-Sulfur Clusters