FUR E.Coli
Description
Product Specs
Product Science Overview
The Ferric Uptake Regulator (Fur) is a DNA-binding protein that plays a crucial role in the regulation of iron homeostasis in Escherichia coli (E. coli). It is a global transcriptional repressor that controls the expression of iron-responsive genes, ensuring that the bacterial cell maintains an optimal balance of iron, which is essential for various cellular processes.
The Fur protein has a molecular mass of approximately 17 kDa . It functions by binding to specific DNA sequences known as Fur boxes, which are located in the promoter regions of target genes. In the presence of sufficient iron, Fur binds to these Fur boxes and represses the transcription of genes involved in iron uptake and storage . This repression prevents the over-accumulation of iron, which can lead to oxidative stress and cellular damage.
Fur operates as a repressor by utilizing ferrous ions (Fe²⁺) as co-repressors. When intracellular iron levels are high, Fur binds to Fe²⁺ and undergoes a conformational change that allows it to bind to the Fur box sequences on the DNA. This binding inhibits the transcription of iron acquisition genes, thereby reducing iron uptake . Conversely, under iron-depleted conditions, Fur is unable to bind to the DNA, leading to the de-repression of these genes and increased iron uptake to meet the cellular demand .
Iron is a vital element for many biological processes, including respiration, DNA synthesis, and metabolism. However, free iron can catalyze the formation of reactive oxygen species (ROS), which can damage cellular components. Therefore, the regulation of iron homeostasis by Fur is critical for the survival and growth of E. coli .
Fur also plays a role in the regulation of other physiological pathways, such as oxidative stress response and virulence. By controlling the expression of genes involved in these pathways, Fur helps E. coli adapt to varying environmental conditions and enhances its pathogenic potential .
Recombinant Fur protein is produced by cloning the fur gene into an expression vector and transforming it into a suitable host, such as E. coli. The recombinant protein can then be purified and used for various research applications, including studies on iron regulation, protein-DNA interactions, and the development of antimicrobial agents targeting iron homeostasis .
