ErpA, an iron–sulfur (Fe–S) protein of the A-type essential for respiratory metabolism in Escherichia coli

Abstract

Understanding 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. Remarkably, erpA was found essential for growth of E. coli in the presence of oxygen or alternative electron acceptors. It was concluded that isoprenoid biosynthesis was impaired by the erpA mutation. First, the eukaryotic mevalonate-dependent pathway for biosynthesis of isopentenyl diphosphate restored the respiratory defects of an erpA mutant. Second, the erpA mutant contained a greatly reduced amount of ubiquinone and menaquinone. Third, ErpA bound Fe-S clusters and transferred them to apo-IspG, a protein catalyzing isopentenyl diphosphate biosynthesis in E. coli. Surprisingly, the erpA gene maps at a distance from any other Fe-S biogenesis-related gene. ErpA is an A-type Fe-S protein that is characterized by an essential role in cellular metabolism.essential gene yadR ͉ isoprenoid ͉ respiration ͉ scaffold

Specialized Function of Yeast Isa1 and Isa2 Proteins in the Maturation of Mitochondrial [4Fe-4S] Proteins

“…Escherichia coli harbors three canonical A-type proteins, IscA, SufA, and ErpA, and the non-canonical NfuA. Deletion of iscA is not associated with a clear phenotype, whereas that of ErpA or a double deletion of iscA and sufA results in strong growth defects (26,27). These phenotypes frequently aggravate under special growth conditions, such as iron limitation or oxidative stress, and are linked to the loss of function of crucial cellular Fe/S proteins (3, 21, 26 -33).…”

Evolution of Fe/S cluster biogenesis in the anaerobic parasite Blastocystis

“…A vector expressing the BhSufCB protein was introduced in two E. coli strains: one carrying the lacZ reporter gene fused to a gene whose expression is repressed by the Fe/S bound form of IscR, iscR (piscR::lacZ); and the second one carrying the lacZ reporter gene fused to hmpA gene (phmpA::lacZ), whose expression is repressed by the Fe/S-bound form of NsrR (SI Appendix) (23,24). Both strains were defective for ISC (ΔiscAU) and SUF (ΔsufCD) biogenesis pathways, and contain the eukaryotic mevalonate-dependent pathway that does not depend on Fe/S enzymes (25). These strains are incapable of synthesizing Fe/S clusters, and thus IscR and NsrR both remain in their "apo" form (i.e., lacking Fe/S cluster), and thus they do not block the transcription of piscR::lacZ and phmpA::lacZ fusions, respectively (SI Appendix, Fig.…”

Bacterial ApbC Protein Has Two Biochemical Activities That Are Required for in Vivo Function

“…Examples include the following: CyaY, an iron-binding protein believed to be involved in iron trafficking and iron delivery (5-7); YggX, an Fe 2ϩ -binding protein that protects the cell from oxidative stress (8,9); ErpA, an alternate A-type [Fe-S] cluster scaffolding protein (10); NfuA, a proposed intermediate [Fe-S] delivery protein (11)(12)(13); YtfE, a protein proposed to be involved in [Fe-S] cluster repair (14,15); and CsdA-CsdE, an alternative cysteine desulferase (16).…”