Molecular organization, biochemical function, cellular role and evolution of NfuA, an atypical Fe-S carrier. - Archive ouverte HAL Access content directly
Journal Articles Molecular Microbiology Year : 2012

Molecular organization, biochemical function, cellular role and evolution of NfuA, an atypical Fe-S carrier.

Abstract

Biosynthesis 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. Phylogenomic analysis allowed us to define four subfamilies. Escherichia coli NfuA is within subfamily II. Most members of this subfamily have a Nfu domain fused to a 'degenerate' A-type carrier domain (ATC*) lacking Fe-S cluster co-ordinating Cys ligands. The Nfu domain binds a [4Fe-4S] cluster while the ATC* domain interacts with NuoG (a complex I subunit) and aconitase B (AcnB). In vitro, holo-NfuA promotes maturation of AcnB. In vivo, NfuA is necessary for full activity of complex I under aerobic growth conditions, and of AcnB in the presence of superoxide. NfuA receives Fe-S clusters from IscU/HscBA and SufBCD scaffolds and eventually transfers them to the ATCs IscA and SufA. This study provides significant information on one of the Fe-S biogenesis factors that has been often used as a building block by ISC and/or SUF synthesizing organisms, including bacteria, plants and animals.

Dates and versions

hal-01054360 , version 1 (06-08-2014)

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Béatrice Py, Catherine Gerez, Sandra Angelini, Rémy Planel, Daniel Vinella, et al.. Molecular organization, biochemical function, cellular role and evolution of NfuA, an atypical Fe-S carrier.. Molecular Microbiology, 2012, 86 (1), pp.155-71. ⟨10.1111/j.1365-2958.2012.08181.x⟩. ⟨hal-01054360⟩
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