Skip to Main content Skip to Navigation
New interface
Journal articles

The ErpA/NfuA complex builds an oxidation-resistant Fe-S cluster delivery pathway

Abstract : 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.
Complete list of metadata

Cited literature [47 references]  Display  Hide  Download
Contributor : Delphine LEROI Connect in order to contact the contributor
Submitted on : Monday, November 12, 2018 - 3:06:52 PM
Last modification on : Thursday, November 10, 2022 - 4:36:14 AM
Long-term archiving on: : Wednesday, February 13, 2019 - 3:59:50 PM


FULL NfuA JBC revised 0903.pdf
Files produced by the author(s)


Distributed under a Creative Commons Attribution 4.0 International License



Beatrice Py, Catherine Gerez, Allison Huguenot, Claude Vidaud, Marc Fontecave, et al.. The ErpA/NfuA complex builds an oxidation-resistant Fe-S cluster delivery pathway. Journal of Biological Chemistry, 2018, 293 (20), pp.7689 - 7702. ⟨10.1074/jbc.RA118.002160⟩. ⟨hal-01915442⟩



Record views


Files downloads