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.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Baez, Andrew Steven

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042117-120835

Advisor

• Argüello, José M.

Year

• 2017

Date created

• 2017-04-21

Resource type

• Major Qualifying Project

Major

• Biochemistry

Rights statement

• In Copyright