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Maria Spies Assistant Professor of Biochemistry and Biophysics Ph.D. 2000, Osaka University, Japan Biochemical mechanisms and function of DNA helicases and DNA motor proteins; protein-nucleic acids and protein-protein interactions; homologous genetic recombination; DNA repair; molecular motors. Maria Spies 493 RAL, MC-712 600 S. Mathews Ave Urbana, IL 61801 217-244-9493 mspies@life.illinois.edu

Current research in my lab focuses on understanding of the molecular mechanisms and cellular functions of DNA helicases (molecular motors that convert chemical energy of ATP binding and hydrolysis into mechanical work of unidirectional translocation along DNA molecule and unwinding of duplex DNA to form ssDNA). DNA helicases are ubiquitous enzymes whose activity is critical for virtually every aspect of DNA metabolism (including DNA repair, recombination, replication and transcription). Hence, mutation in several genes encoding DNA helicases are directly connected to the human genome instability disorders, cancer and aging.

The current major projects in my laboratory involve two recently discovered human helicases: BACH1 and Fbh1. Activity of these enzymes may play an important role in the repair of deleterious two-strand DNA lesions through the process of homologous recombination.

We employ a broad spectrum of experimental techniques including steady-state and pre-steady-state kinetics, structure-functional analysis of protein-DNA and protein-protein interaction, and in vitro reconstitution of the various stages in the processes of DNA repair and recombination.

We use these techniques to understand the biochemical mechanisms and biological functions of the selected helicases. Our analysis is set to answer a number of fundamental mechanistic questions: on which nucleic acids can the enzyme translocate?; what structures does it unwind?; is the enzyme a processive motor?; and how is ATP binding and hydrolysis coupled to translocation along and unwinding of nucleic acids?; We are also working to define the immediate interacting partners for BACH1 and Fbh1 helicases, and to reconstitute in vitro the DNA processing events orchestrated by these enzymes acting in a context of larger macromolecular machines.