Faculty Advisor

Arguello, Jose' M

Abstract

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.

Publisher

Worcester Polytechnic Institute

Date Accepted

December 2008

Major

Biochemistry

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Chemistry and Biochemistry

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