title: Assembly of Fe/S proteins in bacterial systems: Biochemistry of the bacterial ISC system.
abstract: Iron/sulfur clusters are key cofactors in proteins involved in a large number of conserved cellular processes, including gene expression, DNA replication and repair, ribosome biogenesis, tRNA modification, central metabolism and respiration. Fe/S proteins can perform a wide range of functions, from electron transfer to redox and non-redox catalysis. In all living organisms, Fe/S proteins are first synthesized in an apo-form. However, as the Fe/S prosthetic group is required for correct folding and/or protein stability, Fe/S clusters are inserted co-translationally or immediately after translation by specific assembly machineries. These systems have been extensively studied over the last decade, both in prokaryotes and eukaryotes. The present review covers the basic principles of the bacterial housekeeping Fe/S biogenesis ISC system, and related recent molecular advances. Some of the most exciting recent highlights relating to this system include structural and functional characterization of binary and ternary complexes involved in Fe/S cluster formation on the scaffold protein IscU. These advances enhance our understanding of the Fe/S cluster assembly mechanism by revealing essential interactions that could never be determined with isolated proteins and likely are closer to an in vivo situation. Much less is currently known about the molecular mechanism of the Fe/S transfer step, but a brief account of the protein-protein interactions involved is given. This article is part of a Special Issue entitled: Fe/S proteins: Analysis, structure, function, biogenesis and diseases.
authors.affiliation: Université Grenoble Alpes, LCBM, 38054 Grenoble, France; CEA, DSV, iRTSV, LCBM, Biocatalyse, 38054 Grenoble, France; CNRS UMR5249, LCBM, 38054 Grenoble, France.
authors.forename: B
authors.initials: B
authors.lastname: Blanc
authors.affiliation: Université Grenoble Alpes, LCBM, 38054 Grenoble, France; CEA, DSV, iRTSV, LCBM, Biocatalyse, 38054 Grenoble, France; CNRS UMR5249, LCBM, 38054 Grenoble, France.
authors.forename: C
authors.initials: C
authors.lastname: Gerez
authors.affiliation: Université Grenoble Alpes, LCBM, 38054 Grenoble, France; CEA, DSV, iRTSV, LCBM, Biocatalyse, 38054 Grenoble, France; CNRS UMR5249, LCBM, 38054 Grenoble, France. Electronic address: sollagnier@cea.fr.
authors.forename: S
authors.initials: S
authors.lastname: Ollagnier de Choudens
mesh_terms: D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D023061:Gene Order; D007501:Iron / Q000737:chemistry / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008958:Models, Molecular; D009876:Operon; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D029968:Escherichia coli Proteins; D007506:Iron-Sulfur Proteins; D007501:Iron
keywords: Fe/S assembly; Fe/S transfer; Frataxin; Iron–sulfur; Protein complex; Protein–protein interaction