Arguello, Jose' M.
Cu+ is a vital element for cellular functions as it is a cofactor for essential enzymes. At high concentrations, it can be toxic to cells through Fenton-like chemistry. Pressuring cells to regulate the amount of Cu+ by exporting it or storing it in a protein. Recently, a copper storage protein, Csp1, was identified in the methanobacteria. Here, its homologue in Pseudomonas aeruginosa, an opportunistic pathogen, was studied. To understand its role, the construction of expression and mutant/complemented strains of the csp1 gene was attempted. The transcription of csp1 in response to Cu+ and related stress conditions was tested using RT-qPCR. The results showed that transcription of csp1 remained constant under Cu+ toxic levels, suggesting Csp1 might not play a role in Cu+ detoxification.
Worcester Polytechnic Institute
Major Qualifying Project
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Chemistry and Biochemistry