Cu+-ATPases are involved in efflux of Cu+ from the cytoplasm. In vivo, these ATPases receive metal from a specific chaperone. We hypothesize the specificity of the interaction is provided by electrostatic interactions between the transporter and its chaperone. If there are polar amino acids that lie around the Cu+ binding residues of the chaperone, they could potentially interact with the transporter during Cu+ delivery. I used a model system with a Cu+ chaperone (Archaeoglobus fulgidus CopZ) and analyzed the effects on the ATPase activity of its respective transporter (CopA). I made mutants in CopZ that replaced polar residues (Asp, Ser, Thr, and Tyr) and measured its effect on the activation of CopA. There appears to be no effect on activity when the Asp is replaced with an Ala or a Lys.

• 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

• Kaufman, Brad Michael

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-121808-174409

Advisor

• Argüello, José M.

Year

• 2008

Date created

• 2008-12-18

Resource type

• Major Qualifying Project

Major

• Biochemistry

Rights statement

• In Copyright

Last modified

• 2021-01-27