Associate Professor - Ph.D., Washington University
Office: (314) 977-3924
Fax: (314) 977-3658
Mail: Department of Biology, St. Louis University, 3507 Laclede Ave. St. Louis, MO 63103-2010
Courses: General Physiology, Principles of Genetics, Molecular Biology, Cellular and Molecular Genetics
Research Interests: My recent research has focused on the regulation of mitochondrial proliferation and metabolism in the heart, with an emphasis on the role of the transcriptional coactivator peroxisome proliferator-activated receptor g coactivator-1a (PGC-1a) and its interaction with nuclear respiratory factor 1 (NRF-1). Using an inducible, cardiac-specific PGC-1a transgene, we showed that overexpression of PGC-1a induces mitochondrial biogenesis in neonatal mice, but causes cardiomyopathy in adult mice (Circ. Res. 94:525-533, 2004). More recent work has employed overexpression of PGC-1a and NRF-1 in primary cardiac myocytes cultures to delineate NRF-1-dependent pathways downstream of PGC-1a.
Bennett MJ, Russell LK, Tokunaga C, Narayan SB, Tan L, Seegmiller A, Boriack RL, and Strauss AW.Â Reye-like syndrome resulting from novel missense mutations in mitochondrial medium- and short- chain L-3-hydroxy-acyl-CoA dehydrogenase.Â Molecular Genetics and Metabolism 89:74-79 (2006).
Russell LK, Mansfield CM, Lehman JJ, Kovacs A, Courtois M, Saffitz JE, Medeiros DM, Valencik ML, McDonald JA, and Kelly DP.Â Cardiac-Specific Induction of the Transcriptional Coactivator Peroxisome Proliferator-Activated Receptor g Coactivator-1a Promotes Mitochondrial Biogenesis and Reversible Cardiomyopathy in a Developmental Stage-Dependent Manner.Â Circulation Research 94: 525 â€" 533 (2004).
Barycki JJ, Oâ€™Brien LK, Strauss AW, and Banaszak LJ.Â Glutamate 170 of the catalytic dyad of human L-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme.Â Journal of Biological Chemistry 276, 36718-36726 (2001).
Barycki JJ, Oâ€™Brien LK, Strauss AW, and Banaszak LJ.Â Sequestration of the active site by interdomain shifting.Â Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase.Â Journal of Biological Chemistry 275, 27186-27196 (2000).
Barycki JJ, O'Brien LK, Strauss AW, and Banaszak LJ.Â Pig heart short chain L-3-hydroxyacyl-CoA dehydrogenase revisited: sequence analysis and crystal structure determination.Â Protein Science 8, 2010-2018 (1999).
Barycki JJ, O'Brien LK, Bratt JM, Zhang R, Sanishvili R, Strauss AW, and Banaszak LJ.Â Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxycyl-CoA dehydrogenase provide insights into catalytic mechanism.Â Biochemistry 38, 5786-5798 (1999).