Donald Ruhl

Dr. Ruhl is an Associate Professor in the Department of Biochemistry and Molecular Biology and researches the impact of chromatin structure on epigenetic regulation as it relates to organisms and disease. After obtaining a degree in Chemistry from the University of Missouri – St. Louis he attended graduate school at Saint Louis University School of Medicine where he joined the laboratory of Dr. John Chrivia and studied the mechanism of transcriptional regulation mediated by the estrogen receptor and the hormone estrogen. This process is of biological interest due to its link to breast cancer. After receiving a PhD in Pharmacology and Physiology, he joined the laboratory of Dr. W. Lee Kraus at Cornell University where he did his postdoctoral work. As a postdoctoral fellow, he studied the biophysical and biochemical regulation of chromatin structure in response to the estrogen receptor-estrogen complex. He joined Oklahoma State University in 2010.

Research Interests:

In the Ruhl lab, we are interested in understanding how DNA, the molecular blueprint of an organism, is properly read and maintained. Errors in this process lead to disease, most notably cancers. Although a broad range of proteins are involved in this process, we are interested in the Swi/Snf chromatin remodeling complex due to the presence of several tumor suppressors. Using a variety of biochemical and cell-based approaches, we seek knowledge into the link between Swi/Snf function and cancer development. Insight into these processes will aid in the intelligent design of therapeutic drugs that target tumors arising from aberrations in Swi/Snf function. Epigenomic information defines unique patterns of gene expression to maintain cellular identity in an organism. Research into epigenetic mechanisms, including DNA methylation, nucleosome positioning, histone modifications and histone variant deposition, has identified aberrations within these programs that contribute alterations in gene expression that can manifest as an oncogenic phenotype, i.e. a change in cellular identity. Of particular interest is the molecular mechanisms of ATP-dependent remodeling complexes in the accurate positioning of nucleosomes to further understand causality in cancers and aid in the expansion of treatment options. Through the application of biochemical, cell based and genomic approaches in mammalian-based systems, I am interested in understanding the process of nucleosome positioning in both the normal and diseased states.