Research Interests

Understanding the biochemical mechanisms of multi-component ATP-dependent cellular machines required for DNA replication, protein remodeling, and protein degradation has been my long-term scientific goal. Our current research is focused on the mechanism of action of ATP-dependent molecular chaperones and the role of chaperones in proteolysis. Molecular chaperones are present in all organisms and are highly conserved. They mediate protein remodeling, folding, unfolding, assembly, and disassembly without themselves being part of the final complex. Chaperones participate in many fundamental cellular processes including DNA replication, regulation of gene expression, cell division, membrane translocation, protein folding, and protein degradation. Many are induced by environmental stresses and play a critical role during cell stress by preventing the appearance of folding intermediates that lead to irreversibly damaged proteins. They assist in the recovery from stress by refolding and reactivating damaged proteins and by disaggregating aggregated proteins. Some chaperones interact with specific proteolytic components forming compartmentalized ATP-dependent proteases. When associated with proteases, chaperones function in the delivery of damaged proteins and regulatory proteins to the proteolytic component. Molecular chaperones are of fundamental biological importance and are medically relevant, since a number of diseases are caused by aberrant protein folding reactions.

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Primary Section

Section 21: Biochemistry

Secondary Section

Section 26: Genetics