The synthesis and trafficking of iron-sulfur (Fe-S) clusters in both prokaryotes and eukaryotes requires coordination within an expanding network of proteins that function in the cytosol, nucleus, mitochondria, and chloroplasts in order to assemble and deliver these ancient and essential cofactors to a wide variety of Fe-S-dependent enzymes and proteins. This review focuses on the evolving roles of two ubiquitous classes of proteins that operate in this network: CGFS glutaredoxins and BolA proteins. Monothiol or CGFS glutaredoxins possess a Cys-Gly-Phe-Ser active site that coordinates an Fe-S cluster in a homodimeric complex. CGFS glutaredoxins also form [2Fe-2S]-bridged heterocomplexes with BolA proteins, which possess an invariant His and an additional His or Cys residue that serve as cluster ligands. Here we focus on recent discoveries in bacteria, fungi, humans, and plants that highlight the shared and distinct roles of CGFS glutaredoxins and BolA proteins in Fe-S cluster biogenesis, Fe-S cluster storage and trafficking, and Fe-S cluster signaling to transcriptional factors that control iron metabolism--.

原核生物和真核生物中铁硫 (Fe-S) 簇的合成和运输需要在不断扩大的蛋白质网络中进行协调，这些蛋白质在细胞质、细胞核、线粒体和叶绿体中发挥作用，以便组装和传递这些古老而重要的辅助因子到各种铁硫依赖性酶和蛋白质。本综述重点关注在该网络中运行的两种普遍存在的蛋白质类别的演变作用：CGFS 谷氧还蛋白和 BolA 蛋白质。Monothiol 或 CGFS 谷氧还蛋白具有 Cys-Gly-Phe-Ser 活性位点，可在同二聚体复合物中协调 Fe-S 簇。CGFS 谷氧还蛋白还与 BolA 蛋白形成 [2Fe-2S] 桥连的异源复合物，BolA 蛋白具有不变的 His 和一个额外的 His 或 Cys 残基，用作簇配体。