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Bacteria repair damaged clusters in a process that does not require\n            <jats:italic>de novo<\/jats:italic>\n            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 in\n            <jats:italic>cyaY<\/jats:italic>\n            or\n            <jats:italic>yggX<\/jats:italic>\n            were not associated with phenotypic changes in\n            <jats:named-content content-type=\"genus-species\">Escherichia coli<\/jats:named-content>\n            and\n            <jats:named-content content-type=\"genus-species\">Salmonella enterica<\/jats:named-content>\n            serovar Typhimurium, suggesting that CyaY and YggX might have functionally redundant roles. However, we have found that individual mutations in\n            <jats:italic>cyaY<\/jats:italic>\n            or\n            <jats:italic>yggX<\/jats:italic>\n            confer enhanced susceptibility to hydrogen peroxide in\n            <jats:named-content content-type=\"genus-species\">Salmonella enterica<\/jats:named-content>\n            serovar Typhimurium. In addition, inactivation of the\n            <jats:italic>stm3944<\/jats:italic>\n            open reading frame, which is located immediately upstream of\n            <jats:italic>cyaY<\/jats:italic>\n            and which encodes a putative inner membrane protein, dramatically enhances the hydrogen peroxide sensitivity of a\n            <jats:italic>cyaY<\/jats:italic>\n            mutant. Overexpression of STM3944 reduces the elevated intracellular free iron levels observed in an\n            <jats:italic>S<\/jats:italic>\n            . Typhimurium\n            <jats:italic>fur<\/jats:italic>\n            mutant and also reduces the total cellular iron content under conditions of iron overload, suggesting that the\n            <jats:italic>stm3944<\/jats:italic>\n            -encoded protein may mediate iron efflux. Mutations in\n            <jats:italic>cyaY<\/jats:italic>\n            and\n            <jats:italic>yggX<\/jats:italic>\n            have different effects on the activities of the iron-sulfur cluster-containing aconitase, serine deaminase, and NADH dehydrogenase I enzymes of\n            <jats:italic>S<\/jats:italic>\n            . Typhimurium under basal conditions or following recovery from oxidative stress. In addition,\n            <jats:italic>cyaY<\/jats:italic>\n            and\n            <jats:italic>yggX<\/jats:italic>\n            mutations have additive effects on 6-phosphogluconate dehydratase-dependent growth during nitrosative stress, and a\n            <jats:italic>cyaY<\/jats:italic>\n            mutation reduces\n            <jats:named-content content-type=\"genus-species\">Salmonella<\/jats:named-content>\n            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.\n            <jats:named-content content-type=\"genus-species\">Salmonella<\/jats:named-content>\n            experiences oxidative and nitrosative stress within host phagocytes, and CyaY-dependent maintenance of labile iron-sulfur clusters appears to be important for\n            <jats:named-content content-type=\"genus-species\">Salmonella<\/jats:named-content>\n            virulence.\n          <\/jats:p>","DOI":"10.1128\/iai.01022-13","type":"journal-article","created":{"date-parts":[[2014,1,14]],"date-time":"2014-01-14T05:32:51Z","timestamp":1389677571000},"page":"1390-1401","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":39,"title":["Distinct Roles of the Salmonella enterica Serovar Typhimurium CyaY and YggX Proteins in the Biosynthesis and Repair of Iron-Sulfur Clusters"],"prefix":"10.1128","volume":"82","author":[{"given":"Jyoti","family":"Velayudhan","sequence":"first","affiliation":[{"name":"Department of Laboratory Medicine, University of Washington School of Medicine, Seattle, Washington, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joyce E.","family":"Karlinsey","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Washington School of Medicine, Seattle, Washington, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elaine R.","family":"Frawley","sequence":"additional","affiliation":[{"name":"Department of Laboratory Medicine, University of Washington School of Medicine, Seattle, Washington, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lynne A.","family":"Becker","sequence":"additional","affiliation":[{"name":"Department of Laboratory Medicine, University of Washington School of Medicine, Seattle, 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