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Expression of a newly discovered protein involved in iron metabolism
From a search of sequence databases, we have found an interesting protein in archaebacteria that looks like it may be important to
this cell´s iron metabolism. One domain is homologous to a
recently-identified yeast vacuolar iron transport protein. This domain includes several transmembrane helices. From the sequence of the other domain we can tell it belongs to the family of di-iron carboxylate proteins. Our lab has studied this group of proteins for many years, and this family includes ribonucleotide reductase, methane monooxygenase, and the alternative oxidase.
This project involves cloning the gene and expressing the protein in E.coli. We have recently cloned a number of other membrane-bound di-iron carboxylate proteins and we have developed a range of technical tools to apply to this task. Once the protein is expressed, we will study the enzyme/transport activity and crystallize the protein for a structure determination.
This project provides a good opportunity to gain skills in molecular biology (cloning and sequencing DNA) and protein biochemistry (polyacrylamide gel electrophoresis, western immunoblotting) as well as a chance to begin work on a very unique, new protein in iron metabolism.
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