Publications by authors named "Catherine Gerez"
Article Synopsis
- Iron-sulfur (Fe-S) clusters are crucial for various biological processes, including electron transfer and catalysis, and their biosynthesis is supported by specialized protein complexes in all organisms.
- The study focuses on characterizing the native Fe-S cluster in the SufBCD scaffold using multiple spectroscopic techniques, revealing the presence of a [2Fe-2S] cluster and a mysterious second species.
- It suggests that the proteins SufB and SufD contribute to the formation of the [2Fe-2S] cluster, which is transferable to ferredoxin, highlighting its role in the biosynthesis of Fe-S clusters.
Fe-S cluster-containing proteins occur in most organisms, wherein they assist in myriad processes from metabolism to DNA repair via gene expression and bioenergetic processes. Here, we used both and methods to investigate the 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-lives, depending on the carriers they were bound to; an NfuA-bound Fe-S cluster was more stable ( = 100 min) than those bound to SufA ( = 55 min), ErpA ( = 54 min), or IscA ( = 45 min).
View Article and Find Full Text PDFBiosynthesis of iron-sulphur (Fe-S) proteins is catalysed by multi-protein systems, ISC and SUF. However, 'non-ISC, non-SUF' Fe-S biosynthesis factors have been described, both in prokaryotes and eukaryotes. Here we report in vitro and in vivo investigations of such a 'non-ISC, non SUF' component, the Nfu proteins.
View Article and Find Full Text PDFIron/sulfur (Fe/S) proteins are central to the functioning of cells in both prokaryotes and eukaryotes. Here, we show that the yhgI gene, which we renamed nfuA, encodes a two-domain protein that is required for Fe/S biogenesis in Escherichia coli. The N-terminal domain resembles the so-called Fe/S A-type scaffold but, curiously, has lost the functionally important Cys residues.
View Article and Find Full Text PDFUnderstanding the biogenesis of iron-sulfur (Fe-S) proteins is relevant to many fields, including bioenergetics, gene regulation, and cancer research. Several multiprotein complexes assisting Fe-S assembly have been identified in both prokaryotes and eukaryotes. Here, we identify in Escherichia coli an A-type Fe-S protein that we named ErpA.
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