James L. Keck
 |
Associate Professor
Office: (608) 263-1815 |
Education
- B.S. 1992, University of Massachusetts;
- Ph.D. 1997, University of California-Berkeley (S. Marqusee);
- Postdoctoral, 1997-98, Harvard University (J. Wang);1999-01, University of California-Berkeley (J. Berger).
Honors & Awards
- Jane Coffin Childs Memorial Fund Postdoctoral Fellow, 1997-2000;
- Shaw Scientist Award, 2003
Research Interests
Historically, studies of DNA replication, recombination, and repair have been divided into separate research fields, while the connections between these areas have been largely overlooked. However, it is now apparent that these genomic maintenance processes overlap extensively, sharing common enzyme factors and pathways. My lab’s broad research interest is to characterize the mechanisms that coordinate and regulate these processes. Our experimental approach combines enzymology, biochemistry, and X-ray crystallography to study the structure and function of proteins that are involved in multiple nucleic acid metabolic pathways. One project in the lab focuses on the RecQ family of DNA helicases. RecQ proteins have been identified in a variety of species (e.g., E. coli RecQ, S. cerevisiae Sgs1, human WRN and BLM) and have been implicated in a wide range of activities, including replication, recombination, repair, and cellular aging. Mutations in the human genes for RecQ helicases are associated with Werner's, Bloom's and Rothmund-Thompson's syndromes. Thus, the functions of these helicases have a direct impact on human health. Our lab is using bacterial RecQ as a model system to study the mechanisms used by RecQ helicases in their reactions. Our approach includes crystallographic and biochemical experiments to examine the structure-function relationship that supports DNA unwinding activity in RecQ. In addition, we are investigating the roles of other proteins that function with RecQ in the cell.
A second project in the lab examines the molecular basis of the extreme radiation resistance of Deinococcus radiodurans. D. radiodurans can survive massive amounts of radiation that literally shears its genome into hundreds of pieces by non-mutagenically stitching its DNA back together. Several lines of evidence indicate that the bacterium uses multiple mechanisms to accomplish this feat and we are attempting to construct physical/biochemical models that account for its myriad DNA-damage repair pathways. These models rely on findings from our lab as well as from several collaborators efforts. Our hope is that insights from the unusually robust DNA-damage repair mechanisms in D. radiodurans will shed new light onto common mechanisms used in all organisms.
Publications of Note
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University
of Wisconsin - Department
of Biomolecular Chemistry
First published: 01/01/05 Last updated:
1/18/05 Email Biomolecular Chemistry
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