Lee Jin-Won, Helmann John D
Department of Microbiology, Cornell University, Wing Hall, Ithaca, NY 14853-8101, USA.
Biometals. 2007 Jun;20(3-4):485-99. doi: 10.1007/s10534-006-9070-7. Epub 2007 Jan 10.
The ferric uptake regulator (Fur) protein, as originally described in Escherichia coli, is an iron-sensing repressor that controls the expression of genes for siderophore biosynthesis and iron transport. Although Fur is commonly thought of as a metal-dependent repressor, Fur also activates the expression of many genes by either indirect or direct mechanisms. In the best studied model systems, Fur functions as a global regulator of iron homeostasis controlling both the induction of iron uptake functions (under iron limitation) and the expression of iron storage proteins and iron-utilizing enzymes (under iron sufficiency). We now appreciate that there is a tremendous diversity in metal selectivity and biological function within the Fur family which includes sensors of iron (Fur), zinc (Zur), manganese (Mur), and nickel (Nur). Despite numerous studies, the mechanism of metal ion sensing by Fur family proteins is still controversial. Other family members use metal catalyzed oxidation reactions to sense peroxide-stress (PerR) or the availability of heme (Irr).
铁摄取调节蛋白（Fur）最初是在大肠杆菌中发现的，它是一种铁感应阻遏物，可控制铁载体生物合成和铁转运相关基因的表达。尽管Fur通常被认为是一种金属依赖性阻遏物，但它也通过间接或直接机制激活许多基因的表达。在研究最深入的模型系统中，Fur作为铁稳态的全局调节因子，控制铁摄取功能的诱导（在铁限制条件下）以及铁储存蛋白和铁利用酶的表达（在铁充足条件下）。我们现在认识到，Fur家族在金属选择性和生物学功能方面存在巨大差异，其中包括铁（Fur）、锌（Zur）、锰（Mur）和镍（Nur）的传感器。尽管有大量研究，但Fur家族蛋白感应金属离子的机制仍存在争议。其他家族成员利用金属催化氧化反应来感应过氧化物应激（PerR）或血红素的可用性（Irr）。
