Mutated Frataxin in Determining the Mechanisms of the Iron-Sulfur Cluster Assembly
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Date
2013-11-04
Authors
Hsu, Li-yang
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Abstract
Friedreich’s Ataxia is a neurodegenerative disease that results in dysarthria, muscle weakness, spasticity in the lower limbs, scoliosis, bladder dysfunction, loss of lower limb reflexes, and loss of position and vibration senses6. The cause of this disease is generally associated with reduced levels of the protein frataxin. The deficiency in the mitochondrial iron-binding protein frataxin results in diminished activity of various mitochondrial iron-sulfur proteins and influence energy production in cells5. It is known that frataxin is involved in Fe-S cluster assembly and that it interacts with other scaffold or partner proteins such as Isu1 and IsdI. To further understand the mechanism of frataxin and its role in iron homeostasis, we identified conserved amino acids of the protein that are thought to participate in binding iron and set out to mutate these residues to evaluate changes to frataxin activity. We report here our attempts to generate the frataxin mutant D102H.
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Biochemistry, Friedreich's ataxia, frataxin, Parkinson's Disease, iron regulation dysfunction