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.
Phan, Hoang Anh T., "The Impact of Copper(I) on Zinc-finger Structure & Function: A Focus on Transcription Factor Sp1" (2018). Chemistry Honors Projects. 24.
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