Dr. Brian David Strahl is presently an Associate Professor in the Department of Biochemistry and Biophysics in the School of Medicine at the University of North Carolina at Chapel Hill (UNC-Chapel Hill). He also holds a secondary faculty appointment in UNC’s Lineberger Comprehensive Cancer Center, and is currently the Faculty Director of the High-Throughput Peptide Synthesis and Arraying core facility (UNC HTPSA) and act as the Director of Graduate Studies in his home department.
Brian Strahl studied at the University of North Carolina at Greensboro where he finished his two bachelor’s degrees in Chemistry and Biology in 1993. It was in his college years where he became interested in biological research and became involved in several undergraduate research studies in the Chemistry and Biology Departments. In Chemistry, he studied under the mentorship Dr. Bruce Banks, where he investigated the enzymatic properties of lipase in organic solvents while in Biology, he was mentored by Dr. Julian Lombardi. In Dr. Julian Lombardi’s lab, he discovered a new approach and method to examine the dry mass content of extremely small volumes of biological fluid using a state-of-the-art ultra microbalance. This method allowed the evaluation of nutrients contained in the small volumes of embryonic fluid found in live bearing sharks to study their developmental regulation – for which little was known at the time.
In 1993, Brian Strahl enrolled in the Department of Biochemistry at North Carolina State University to complete his doctorate degree. He studied under the mentorship of Dr. William L. Miller and in his lab Brian sought to understand how the Follicle-Stimulating Hormone-Beta (FSHß) gene is regulated at the transcriptional level. His efforts resulted in a new understanding for how the transcription factor AP-1 mediates FSHß gene activation through PKC. His work also showed that Gonadotropin Releasing Hormone (GnRH) functions to control FSHß gene activation through PKC and AP-1. His work provided new insights into the regulation of this critical hormone. In 1998, Dr. Brian Strahl completed his doctorate degree and then moved on to perform his postdoctoral studies under the mentorship of Dr. C. David Allis at the University of Virginia’s Department of Biochemistry and Molecular Genetics. He contributed to the identification and characterization of lysine and arginine histone methyltransferases. In addition, Dr. Strahl, together with David Allis, coined the ‘Histone Code’ hypothesis – which aimed to provide an explanation for how multiple histone modifications function together to regulate chromatin structure and function.
In December of 2001, Dr. Strahl started his own laboratory at University of North Carolina. His lab is focused on deciphering the role of histone modifications – such as lysine methylation, lysine ubiquitination and lysine acetylation – in chromatin function. Using yeast and human cells as model systems, together with his colleagues, they are determining the role of a number of histone-modifying enzymes and how they contribute to gene regulation and heterochromatin formation. His recent work has discovered how histone H3 lysine 9 methylation is critical for the maintenance of DNA methylation in human cells. Moreover, the Strahl laboratory demonstrated that UHRF1, a E3 ubiquitin ligase, binds to methylated histone H3 using several of its histone-interacting domains to help recruit the DNA maintenance methylase DNMT1. These studies have led to new insights into how combinatorial histone modifications contribute to chromatin function.