734 Riffe Building
496 W 12th Ave
Columbus, OH 43210
Areas of Expertise
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, at http://go.osu.edu/fosterlab.
Protein and nucleic acid structure and dynamics; molecular recognition; gene regulation; enzyme catalysis; NMR spectroscopy; molecular biophysics; thermodynamics; kinetics.
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 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 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.
Crowe BL, Larue RC, Yuan C, Hess S, Kvaratskhelia M, Foster MP. Structure of the Brd4 ET domain bound to a C-terminal motif from γ-retroviral integrases reveals a conserved mechanism of interaction. Proc Natl Acad Sci U S A. 2016 Feb 23;113(8):2086-91. DOI. Epub 2016 Feb 8. PubMed; PubMed Central PMCID: PMC4776507.
Ihms EC, Zhou M, Zhang Y, Kleckner IR, McElroy CA, Wysocki VH, Gollnick P, Foster MP. Gene regulation by substoichiometric heterocomplex formation of undecameric TRAP and trimeric anti-TRAP. Proc Natl Acad Sci U S A. 2014 Mar 4;111(9):3442-7. DOI. Epub 2014 Feb 18. PubMed; PubMed Central PMCID: PMC3948263.
Kleckner IR, McElroy CA, Kuzmic P, Gollnick P, Foster MP. Homotropic cooperativity from the activation pathway of the allosteric ligand-responsive regulatory trp RNA-binding attenuation protein. Biochemistry. 2013 Dec 10;52(49):8855-65. DOI. Epub 2013 Nov 22. PubMed; PubMed Central PMCID: PMC3946311.
Xu Y, Oruganti SV, Gopalan V, Foster MP. "Thermodynamics of Coupled Folding in the Interaction of Archaeal RNase P Proteins RPP21 and RPP29." (2012) Biochemistry 51 (4):926–935. DOI
Kleckner IR, Foster MP. "GUARDD: User-friendly MATLAB software for rigorous analysis of CPMG RD NMR data." (2012) J Biomol NMR 52:11-22. DOI
Kleckner IR, Gollnick P, Foster MP. "Mechanisms of Allosteric Gene Regulation by NMR Quantification of μs-ms Protein Dynamics." (2012) J Mol Biol 415(2): 372-381. DOI
Chen WY, Xu Y, Cho IM, Oruganti SV, Foster MP, Gopalan V. "Cooperative RNP assembly: complementary rescue of structural defects by protein and RNA subunits of archaeal RNase P." (2011) J Mol Biol. 411(2):368-83.DOI (PubMed)
Kleckner IR, Foster MP. "An Introduction to NMR-based Approaches for Measuring Protein Dynamics." (2010) BBA - Proteins and Proteomics. Special Issue: Protein Dynamics.1841(8):942-968 DOI
Sachleben JR, McElroy CA, Gollnick P, Foster MP. "Mechanism for pH-dependent gene regulation by amino-terminus-mediated homooligomerization of Bacillus subtilis anti-trp RNA-binding attenuation protein." (2010) Proc Natl Acad Sci U S A 107(35):15385-90 DOI
Xu Y, Amero CD, Pulukkunat DK, Gopalan V, Foster MP. "Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA interactions." (2009) J Mol Biol. 393(5):1043-55. (PDF, DOI; PubMed)
Amero CD, Byerly DW, McElroy CA, Simmons A, Foster MP. "Ligand-induced changes in the structure and dynamics of Escherichia coli peptide deformylase." (2009) Biochemistry. 48(32):7595-607. DOI (PDF, SI). Addendum.
Amero CD, Boomershine WP, Xu Y, Foster M. "Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner." (2008) Biochemistry. 47(45):11704-10. DOI (PDF)
Kamadurai HB, Jain R and Foster MP, "Crystallization and structure determination of the core-binding domain of bacteriophage lambda integrase." (2008) Acta Crystallographica F, 64(6):470-473. (PDF, DOI)
Amero CD, Arnold JJ, Moustafa IM, Cameron CE, and Foster MP, "Identification of the oriI-binding site of poliovirus 3C protein by NMR spectroscopy." (2008) J Virol, 82(9):4363-70, PMID: 18305026. (PubMed, DOI, PDF)
Subramaniam S, Kamadurai HB, Foster MP, "Trans Cooperativity by a Split DNA Recombinase: The Central and Catalytic Domains of Bacteriophage Lambda Integrase Cooperate in Cleaving DNA Substrates When the Two Domains Are not Covalently Linked." (2007) J Mol Biol. 370(2):303 - 314. (PubMed, PDF) DOI
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