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Access Type

WSU Access

Date of Award

January 2023

Degree Type

Dissertation

Degree Name

Ph.D.

Department

Pharmaceutical Sciences

First Advisor

Timothy L. Stemmler

Abstract

Iron-sulfur clusters are ubiquitous and phylogenetically conserved cofactors that are essential in all kingdoms of life. These cofactors are biosynthesized, in eukaryotes, within the Mitochondrial Iron-Sulfur Cluster Bioassembly, consisting of a multi-protein complex comprised of six dimeric proteins. Of the protein, the focus of this dissertation is frataxin and the scaffold protein. Frataxin is an iron-binding protein that interacts with other assembly proteins and participates in iron delivery to the scaffold protein. The scaffold protein is the protein upon which Fe-S clusters are formed. The interaction of these proteins in one of the many important process necessary to understand cluster assembly, specifically as it relates to the cardio- and neurodegenerative disorder, Friedreich’s ataxia.

The studies previously published, and studies of this project promote the awareness of the Drosophila melanogaster model system being more stable against aggregation and degradation compared to prokaryotic and eukaryotic orthologs alike. Here, we advanced the field by producing the crystal structure of Dfh, determining its iron binding regions, examining the structure of DIsu upon cluster assembly, and the stability of the interactions between DIsu with cluster assembly substrates and Dfh. Studying cluster assembly in a more stable model system will aid in further understanding of the process in a variety of organisms.

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