Document Type

Honors Project On-Campus Access Only


A possible mechanism for copper toxicity and transcriptionally-regulated copper homeostasis entails the displacement of Zn(II) by Cu(I) in zinc-finger (ZF) Specificity Protein 1 – Sp1, which consists of three different ZF domains. In this project, an Sp1 construct that retains DNA binding was successfully purified and characterized. Protein-DNA interactions of Sp1 and metal-binding properties of its individual ZF domains were explored using multiple techniques including electrophoresis, fluorescence, and UV-Vis spectroscopy. The results suggest that Cu(I) disrupts Sp1’s interaction with hCtr1 gene promoter region and that each ZF domain of Sp1 binds one Cu(I) ion with similar affinities.



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