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In our lab, we are using a combination of biochemical, biophysical, and cellular approaches to understand the cellular functions and regulation of the human mitochondrial molecular chaperone mtHsp70. The specific goals of our research are to understand, i. how and why the hsp70 escort protein Hep regulates mtHsp70, ii. whether mtHsp70-mediated Fe/S-cluster biogenesis is subject to distinct regulation from bacterial and yeast chaperones, and iii. what developmental defects arise from mutations in human mitochondrial hsp70 and its auxiliary cochaperones. We are also engineering new tools for metallomics and proteomics. Biosensors are being optimized that can image the 2Fe2S cluster content of proteins in living cells. These sensors are being developed to aid in screening chemical libraries for small molecules that suppress pathologies arising from iron-sulfur cluster synthesis defects, such as myopathies. Genetic selections are also being developed that can measuring protein-protein interactions in hyperthermophiles, organisms that grow optimally near the boiling point of water. These protein-fragment complementation assays are being developed to increase our understanding of the biotechnological potential for thermostable enzymes and to facilitate the engineering of oligomeric, thermostable nanomaterials.
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