Institut Pasteur, Université Paris Cité, CNRS UMR6047, Stress Adaptation and Metabolism Unit, Department of Microbiology, F-75015 Paris, France.
Metallomics. 2022 May 25;14(5). doi: 10.1093/mtomcs/mfac022.
Iron-sulfur (Fe-S) clusters are inorganic ubiquitous and ancient cofactors. Fe-S-bound proteins contribute to most cellular processes, including DNA replication and integrity, genetic expression and regulation, metabolism, biosynthesis, and most bioenergetics systems. Also, Fe-S proteins hold a great biotechnological potential in metabolite and chemical production, including antibiotics. From classic biophysics and spectroscopy methodologies to recent development in bioinformatics, including structural modeling and chemoproteomics, our capacity to predict and identify Fe-S proteins has spectacularly increased over the recent years. Here, these developments are presented and collectively used to update the composition of Escherichia coli Fe-S proteome, for which we predict 181 occurrences, i.e. 40 more candidates than in our last catalog, and equivalent to 4% of its total proteome. Besides, Fe-S clusters can be targeted by redox active compounds or reactive oxygen and nitrosative species, and even be destabilized by contaminant metals. Accordingly, we discuss how cells handle damaged Fe-S proteins, i.e. degradation, recycling, or repair.
铁硫 (Fe-S) 簇是无机、普遍存在且古老的辅因子。Fe-S 结合蛋白参与大多数细胞过程，包括 DNA 复制和完整性、基因表达和调控、代谢、生物合成以及大多数生物能系统。此外，Fe-S 蛋白在代谢物和化学品生产方面具有巨大的生物技术潜力，包括抗生素。从经典的生物物理学和光谱学方法到最近的生物信息学发展，包括结构建模和化学蛋白质组学，我们预测和识别 Fe-S 蛋白的能力在近年来有了显著提高。在这里，介绍了这些发展，并共同用于更新大肠杆菌 Fe-S 蛋白质组的组成，我们预测了 181 个发生事件，即比我们上次的目录多 40 个候选事件，相当于其总蛋白质组的 4%。此外，Fe-S 簇可以被氧化还原活性化合物或活性氧和亚硝态物种靶向，甚至被污染物金属破坏。因此，我们讨论了细胞如何处理受损的 Fe-S 蛋白，即降解、回收或修复。
