Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Biochim Biophys Acta Mol Cell Res. 2021 Jan;1868(1):118847. doi: 10.1016/j.bbamcr.2020.118847. Epub 2020 Sep 7.
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--.
铁硫 (Fe-S) 簇在原核生物和真核生物中的合成和运输需要在一个不断扩大的蛋白质网络中进行协调,该网络在细胞质、核、线粒体和叶绿体中发挥作用,以便将这些古老而必需的辅助因子组装并递送到各种依赖 Fe-S 的酶和蛋白质中。本文重点介绍了在该网络中发挥作用的两类普遍存在的蛋白质的不断发展的作用:CGFS 谷氧还蛋白和 BolA 蛋白。单硫醇或 CGFS 谷氧还蛋白具有一个 Cys-Gly-Phe-Ser 活性位点,在同源二聚体复合物中协调一个 Fe-S 簇。CGFS 谷氧还蛋白还与 BolA 蛋白形成 [2Fe-2S]-桥接异源复合物,BolA 蛋白具有一个不变的 His 和另外一个 His 或 Cys 残基,作为簇配体。在这里,我们重点介绍了细菌、真菌、人类和植物中的最新发现,这些发现突出了 CGFS 谷氧还蛋白和 BolA 蛋白在 Fe-S 簇生物发生、Fe-S 簇储存和运输以及 Fe-S 簇信号转导到控制铁代谢的转录因子中的共享和独特作用。