- Chem Sci 510B
- Associate Professor, Chemistry
- Postdoctoral Fellow, University of Michigan, Ann Arbor, MI
- PhD, Arizona State University, Tempe, AZ
Our multi-disciplinary research program aims to understand the molecular architecture and recognition features of the early events in transcription initiation, and to use these insights to develop inhibitors of transcriptional assembly. A growing number of studies are finding diverse and essential roles for molecular recognition events in mediating information transfer and complex assembly in biology. In fact, biological outcomes are often due to physical interactions between proteins that are so highly selective that seemingly minor chemical modifications (i.e. methylation, acetylation or phosphorylation) can completely abolish biomolecular recognition processes and redirect signaling pathways. In principle, development of small molecule inhibitors of interactions of specific transcriptional activators (or repressors) with DNA or with the basal transcription machinery could provide highly selective regulators of gene expression and thus highly selective therapeutic agents (e.g., antiviral agents based on disabling essential viral gene expression).
Links of Interest
- Understanding the molecular recognition features and assembly mechanisms of gene regulation
- Thompson, M. (2009) Thermodynamic and kinetic analysis of bromodomain-histone interactions. Methods in Enzymology, Biothermodynamics, Part B, 466. In press.
- Thompson, M. (2009) Polybromo-1: the chromatin targeting subunit of the PBAF complex. Biochimie. 91, 309-319.
- Kupitz, C., Chandrasekaran, R., and Thompson, M. (2008) Kinetic analysis of acetylation- dependent Pb1 bromodomain-histone interactions. Biophys. Chem. 136, 7-12.
- Garzón, J.F.G., Kupitz, C., Bailey, J., and Thompson, M. (2008) Acetylation-dependent binding analysis of the yeast Gcn5 bromodomain protein. American Journal of Undergraduate Research 7, 19-26.
- Thompson, M., and Chandrasekaran, R. (2008) Thermodynamic analysis of acetylation- dependent Pb1 bromodomain-histone H3 interactions. Analytical Biochemistry 374, 304-312.
- Chandrasekaran, R., and Thompson, M. (2007) Polybromo-1-bromodomains bind histone H3 at specific acetyl-lysine positions. Biochemical and Biophysical Research Communications 355, 661-666.
- Thompson, M. (2007) Spectral Properties and DNA Targeting Features of a Thiazole Orange- Peptide Bioconjugate. Biomacromolecules 8, 3628 - 3633.
- M. Thompson. A thermodynamic model for acetylation-dependent polybromo-histone interactions. Southeastern Regional Meeting of the American Chemical Society (SERMACS), Nashville, TN, November 12, 2008.
- M. Thompson. Polybromo-1 bromodomains bind histone H3 at specific acetyl-lysine positions. 235th American Chemical Society National Meeting, New Orleans, LA, March 22, 2008.
- K. Bugielski, M. Thompson. Thermodynamic analysis of acetylation-dependent Pb1 bromodomain - histone H3 interactions. 235th American Chemical Society National Meeting, New Orleans, LA, March 21, 2008.
- K. Bugielski, M. Thompson. Methyl-histone binding analysis of the yeast double chromodomain protein Chd1. 235th American Chemical Society National Meeting, New Orleans, LA, March 20, 2008.
- C. Kupitz, M. Thompson. Kinetic analysis of acetylation-dependent Pb1 bromodomain- histone interactions. 235th American Chemical Society National Meeting, New Orleans, LA, March 19, 2008.
- M. Thompson. Deciphering the histone acetylation code for human Polybromo-1. University Northern Michigan, Department of Chemistry, Marquette, Michigan. October 6, 2006. Invited Seminar.
- M. Thompson, R. Chandrasekaran. Deciphering the Histone Acetylation Code for Human Polybromo-1. Great Lakes Regional Meeting of the American Chemical Society, Milwaukee, WI, May 31, 2006.
- US Patent #6,348,317 - Fluorescent and DNA cleavage properties of peptide/dye conjugates. Thompson, M. and Woodbury, N.W. (2001), Arizona State University