Bio

Prof. Mark P. Foster spent his formative years in Maturin, Venezuela, before returning to the US to attend high school in upstate NY. He earned a BS in Chemistry from the University of Illinois, Urbana-Champaign, and a PhD in Natural Products/Medicinal Chemistry from the University of Utah. He received an NIH NRSA postdoctoral award and was American Cancer Society Postdoctoral Fellow in the laboratory of Prof. Peter E. Wright, in the Department of Molecular Biology at The Scripps Research Institute, La Jolla, CA, where he learned to apply high-field NMR spectroscopy to problems in macromolecular structure and function. Dr. Foster’s research has been supported by grants from the American Cancer Society, American Chemical Society/PRF, American Heart Association, Milheim Foundation for Cancer Research, The National Institutes of Health, and he was recipient of a CAREER Award from the National Science Foundation. He has served as Director of the Structural Biology and Molecular Biophysics Division, OSU Biophysics Program, Chair of the Department of Biochemistry, and Vice Chair of the Department of Chemistry and Biochemistry. He has served as ad hoc grant reviewer for many non-profit granting agencies, including the ACS, AHA, NSF, NIH, Science Foundation Ireland, Israel Science Foundation, Swiss National Science Foundation, and Burrows Wellcome Trust, and served as a standing member of NIH molecular biophysics study section MSF-C. He also served on the External Advisory Board for NMRFAM. He is a member of the American Chemical Society, Protein Society and Biophysical Society. At OSU Dr. Foster trains graduate students in Chemistry, Biochemistry and Biophysics, and is a member of the OSU Biophysics Graduate Program, Chemistry-Biology Interface NIH Training Program, and Cellular, Molecular, and Biochemical Sciences NIH Training Program. More information about Dr. Foster’s research interests can be found on his laboratory page.

Research Overview 

Topics

Protein and nucleic acid structure and dynamics; molecular recognition; gene regulation; enzyme catalysis; NMR spectroscopy; molecular biophysics; thermodynamics; kinetics.

Approach

The Foster group uses nuclear magnetic resonance spectroscopy (NMR) and other biochemical and biophysical techniques to understand the structure and function of biological macromolecules, and to decipher the ways in which they recognize and interact with each other. Our group and our collaborators tackle a range of fascinating questions that allow us to understand how genes are regulated (turned “on” or “off”), how enzymes catalyze chemical reactions, or how drug-like molecules bind and inhibit their cellular targets. Such insights are fundamental to understanding biology and for applying that knowledge to problems in medicine or biotechnology. Members of the lab receive both broad training in biochemistry, biophysics and structural biology, and highly focused training centered on their research project and the tools most critical to its advancement. With this combination of broad and deep research training, group members emerge with the scientific skills to pursue careers in a wide variety of settings, from academia to the private sector.

Projects

Projects in the Foster Lab include interaction of retroviral integrases (HIV, MLV) with eukaryotic transcriptional machinery (LEDGF, Brd4), ligand-dependent binding of proteins to nucleic acids (TRAP, Loz1), enzyme dynamics (Cre recombinase, RNase P, ProXp-Ala), and RNA-mediated gene regulation (riboswitches). In partnership with our collaborators, we tackle fascinating research problems in a supportive, exciting and fast-paced learning environment. We invite you to visit the lab web pages (http://go.osu.edu/fosterlab) and contact us if you have questions or are interested in collaborations, or to learn more about our science.

Publications

For a complete list of publications, click here.

Ma X, Baktina M, Shulgina I, Cantara WA, agy ABK, Goto Y, Suga H, Foster MP, Musier-Forsyth K. Structural basis of tRNAPro acceptor stem recognition by a bacterial trans-editing domain. Nucleic Acids Res. 2023 May 8; 51(8):3988-3999. doi: 10.1093/nar/gkad192.

Li W, Norris AS, Lichtenthal K, Kelly S, Ihms EC, Gollnick P, Wysocki VH, Foster MP. Thermodynamic coupling between neighboring binding sites in homo-oligomeric ligand sensing protiens from mass resolved ligand-dependent population distributions. Protein Science 2022 Sept. 27; 31(10): e4424. doi: 10.1002/pro.4424.

Stachowski K, Norris AS, Potter D, Wysocki V, Foster MP. Mechanisms of Cre recombinase synaptic complex assembly and activation illuminated by Cryo-EM. Nucleic Acids Res. 2022 Feb. 1; gkac032. doi: 10.1093/nar/gkac032.

Wagner N, Foster MP. Nearest-Neighbor Effects Modulate loxP Spacer DNA Chemical Shifts and Guide Oligonucleotide Design for Nuclear Magnetic Resonance Studies. Biochem. 2022 Jan. 18; 61(2):67-76. doi: 10.1021/acs.biochem.1c00571.