Terry J. Watt PhD

Education

• B.S. in technical writing, Carnegie Mellon University
• B.S. in chemistry, Carnegie Mellon University
• M.S. in chemistry, Carnegie Mellon University
• Ph.D. in biochemistry, Georgia Institute of Technology (2007)
• Postdoctoral research associate, University of Michigan - Ann Arbor (2008-2010)
• Assistant professor of chemistry, Xavier University of Louisiana (2010-2016)
• Associate professor of chemistry, Xavier University of Louisiana (2016- )

Research Interest

Our research focuses on proteins called lysine deacetylases (KDACs) or histone deacetylases (HDACs).  KDACs chemically modify other cellular proteins, and they have been linked to a wide range of essential cellular behaviors.  Aberrant KDAC activity appears to be linked to numerous disease states, including many cancers.  However, because it is largely unknown which proteins are being modified by KDACs, the reasons for the links to diseases are unclear.  Our goal is to understand the physical interactions between KDACs and other proteins.  Approaches utilized in the lab include characterization of purified KDACs and genetic engineering to control KDAC behavior in cells.  Greater understanding of these interactions, and identification of particular target proteins, may lead to new therapies and diagnostics for diseases via new cellular pathways and drug targets.

Current research areas include:

• identifying substrates of KDACs;
• identifying non-substrate binding partners of KDACs;
• determining the cellular functions of KDACs;
• characterizing specific interactions between KDACs and substrates;
• determining the effects of potential regulating molecules on KDAC activity.

Approaches and techniques used include enzyme kinetics, molecular biology, gene expression analysis, protein spectroscopy, mass spectrometry, molecular modeling, cell culture, and genetic engineering.

Recent Publications

‍Toro TB, Edenfield SA, Hylton BJ, Watt TJ. Chelatable trace zinc causes low, irreproducible KDAC8 activity.  Anal. Biochem. 2018, 540-541, 9-14.  PMID: 29100752

Toro TB, Painter RG, Haynes RA, Glotser EY, Bratton MR, Bryant JR, Nichols KA, Matthew-Onabanjo AN, Matthew AN, Bratcher DR, Perry CD, Watt TJ.  Purification of metal-dependent lysine deacetylases with consistently high activity.  Protein Exp. Purif. 2018, 141, 1-6.  PMID: 28843507

Toro TB, Bryant JR, Watt TJ.  Lysine deacetylases exhibit distinct changes in activity profiles due to fluorophore-conjugation of substrates.  Biochemistry 2017, 56, 4549-4558.  PMID: 28749131

Toro TB, Pingali S, Nguyen TP, Garrett DS, Dodson KA, Nichols KA, Haynes RA, Payton-Stewart F, Watt TJ.  KDAC8 with high basal velocity is not activated by N-acetylthioureas.  PLoS One 2016, 11, e0146900.  PMID: 26745872

Toro TB, Watt TJ.  KDAC8 substrate specificity quantified by a biologically-relevant, label-free deacetylation assay.  Protein Sci. 2015, 24, 2020-2032.  PMID: 26402585

Johanson KE, Watt TJ.  Inquiry-based experiments for large-scale introduction to PCR and restriction enzyme digests.  Biochem. Mol. Bio. Ed. 2015, 43, 441-448.  PMID: 26503481

Toro TB, Nguyen TP, Watt TJ.  An improved 96-well turbidity assay for T4 lysozyme activity.  MethodsX 2015, 2, 256-262.  PMID: 26150996

Johanson KE, Watt TJ, McIntyre NR, Thompson M.  Purification and characterization of enzymes from yeast: an extended undergraduate laboratory sequence for large classes.  Biochem. Mol. Bio. Ed. 2013, 41, 251-261.  PMID: 23868379

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