Regulation of the iron transporter gene fepA is crucial for cell viability

FepA is an Escherichia coli (E. coli) membrane protein which transports the iron-bound siderophore ferric enterobactin from the exterior into the periplasm. Thereby it helps to provide the cells with soluble iron. In the study, its gene, fepA, was ligated into pUC8. E. coli cells were then transformed with this construct and tested for presence and orientation of sense or antisense expression. The majority of colonies that have taken up pUC8 with a fepA fragment were found to contain the gene in antisense orientation. It was concluded that removal of the gene from its regulation leading to its over-expression results in unviable clones possibly due to membrane protein toxicity or iron toxicity.

Klappentext

Research Paper (postgraduate) from the year 2010 in the subject Biology - Genetics / Gene Technology, grade: 1,0, Washington State University, course: Techniques in Molecular Biology, language: English, abstract: FepA is an Escherichia coli (E. coli) membrane protein which transports the iron-bound siderophore ferric enterobactin from the exterior into the periplasm. Thereby it helps to provide the cells with soluble iron. In the study, its gene, fepA, was ligated into pUC8. E. coli cells were then transformed with this construct and tested for presence and orientation of sense or antisense expression. The majority of colonies that have taken up pUC8 with a fepA fragment were found to contain the gene in antisense orientation. It was concluded that removal of the gene from its regulation leading to its over-expression results in unviable clones possibly due to membrane protein toxicity or iron toxicity.