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Proteins containing DUF59 domains have roles in iron-sulfur (FeS) cluster assembly and are widespread throughout Eukarya, Bacteria, and Archaea. However, the function(s) of this domain is unknown.  Staphylococcus aureus  SufT is composed solely of a DUF59 domain. We noted that  sufT  is often co-localized with  sufBC , which encode for the Suf FeS cluster biosynthetic machinery. Phylogenetic analyses indicated that  sufT  was recruited to the  suf  operon, suggesting a role for SufT in FeS cluster assembly. A  S .  aureus  Δ sufT  mutant was defective in the assembly of FeS proteins. The DUF59 protein Rv1466 from  Mycobacterium tuberculosis  partially corrected the phenotypes of a Δ sufT  mutant, consistent with a widespread role for DUF59 in FeS protein maturation. SufT was dispensable for FeS protein maturation during conditions that imposed a low cellular demand for FeS cluster assembly. In contrast, the role of SufT was maximal during conditions imposing a high demand for FeS cluster assembly. SufT was not involved in the repair of FeS clusters damaged by reactive oxygen species or in the physical protection of FeS clusters from oxidants. Nfu is a FeS cluster carrier and  nfu  displayed synergy with  sufT . Furthermore, introduction of  nfu  upon a multicopy plasmid partially corrected the phenotypes of the Δ sufT  mutant. Biofilm formation and exoprotein production are critical for  S .  aureus  pathogenesis and vancomycin is a drug of last-resort to treat staphylococcal infections. Defective FeS protein maturation resulted in increased biofilm formation, decreased production of exoproteins, increased resistance to vancomycin, and the appearance of phenotypes consistent with vancomycin-intermediate resistant  S .  aureus . We propose that SufT, and by extension the DUF59 domain, is an accessory factor that functions in the maturation of FeS proteins. In  S .  aureus , the involvement of SufT is maximal during conditions of high demand for FeS proteins.

plos genetics

The DUF59 Containing Protein SufT Is Involved in the Maturation of Iron-Sulfur (FeS) Proteins during Conditions of High FeS Cofactor Demand in Staphylococcus aureus