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The ErpA/NfuA complex builds an oxidation-resistant Fe-S cluster delivery pathway
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Edité par CCSD ; American Society for Biochemistry and Molecular Biology -
International audience. Fe-S cluster containing proteins occur in most organisms wherein they assist a myriad of diverse processes from metabolism to DNA repair via gene expression and bioenergetic processes. Here we used both in vitro and in vivo methods to investigate capacity of the four Fe-S carriers, NfuA, SufA, ErpA and IscA to fulfill their targeting role under oxidative stress. Likewise, Fe-S clusters exhibited varying half-live depending on the carriers they are bound to: NfuA-bound FeS cluster was more stable (t1/2 100 min) than SufA- (t1/2 55 min), ErpA (t1/2 54 min), and IscA (t1/2 45 min). Surprisingly, presence of NfuA further enhanced stability of the ErpA-bound cluster to t1/2 100 min. Using genetic and plasmon surface resonance analyses, we showed that NfuA and ErpA interacted directly with client proteins whereas IscA/SufA did not. Moreover, NfuA and ErpA interacted one with the other. Given all these observations we propose an architecture of the the Fe-S delivery network in which ErpA is the last factor that delivers cluster directly to most if not all client proteins. NfuA is proposed to assist ErpA under severe unfavorable conditions. Comparison with the strategy employed in yeast and eukaryotes is discussed.
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