title: Iron-sulfur cluster biosynthesis in bacteria: Mechanisms of cluster assembly and transfer.
abstract: Iron-sulfur [Fe-S] clusters are ubiquitous ancient prosthetic groups that are required to sustain fundamental life processes. Formation of intracellular [Fe-S] clusters does not occur spontaneously but requires a complex biosynthetic machinery. Different types of [Fe-S] cluster assembly systems have been discovered. All of them have in common the requirement of a cysteine desulfurase and the participation of [Fe-S] scaffold proteins. The purpose of this review is to discuss various aspects of the molecular mechanisms of [Fe-S] cluster assembly in living organisms: (i) mechanism of sulfur donor enzymes, namely the cysteine desulfurases; (ii) mechanism by which clusters are preassembled on scaffold proteins and (iii) mechanism of [Fe-S] cluster transfer from scaffold to target proteins.
authors.affiliation: CNRS UMR 5249, F-38054 Grenoble, France. mfontecave@cea.fr
authors.forename: Marc
authors.initials: M
authors.lastname: Fontecave
authors.forename: Sandrine
authors.initials: S
authors.lastname: Ollagnier-de-Choudens
mesh_terms: D001419:Bacteria / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D013437:Carbon-Sulfur Lyases / Q000378:metabolism; D003545:Cysteine / Q000378:metabolism; D007501:Iron / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000096:biosynthesis*; D017510:Protein Folding
chemical_list: D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D007501:Iron; D013437:Carbon-Sulfur Lyases; C080546:cysteine desulfurase; D003545:Cysteine