Natosha L. Finley

Natosha L. Finley

Assistant Professor of Micro­biology



Ph.D., University of Cincinnati, 2005

Research Interests:

For more detailed information regarding current research projects in the Finley Lab, click the following link:

Bacterial pathogenesis:

My lab utilizes NMR and molecular biophysics to gain a better understanding of the biological processes that contribute to the development of human diseases. Several important human pathogens such as Bacillus anthracis, Bordetella pertussis, and Pseudomonas aeruginosa make toxins that facilitate the ability of these organisms to infect humans.   One area of interest in the lab is how exotoxins gain access to host cells and the way in which these toxins are activated during infections. A detailed molecular understanding of the interaction between the host cell and bacterial exotoxins may facilitate the rational design of novel therapeutics to combat human pathogens.


NMR-based metabolomics is a powerful tool for characterizing the small molecular weight metabolites generated by living organisms as a consequence of carry out normal life processes. We are using this technique to address the following biological questions:

  1. How do microbiomes interact with their environments?
  2. What metabolites are important biomarkers indicating normal and pathological states in muscles, organs, and tissues?
Muscle Contraction:

Another goal of my research program is to define the molecular basis by which thick filament proteins participate in the control of cardiac muscle contraction. Several naturally occurring mutations in muscle regulatory proteins are linked to progressive forms of heart disease and skeletal muscle abnormalities. By examining the structural and functional consequences of these protein variants, we hope to better understand the transition from normal to diseased states in heart and skeletal muscles. Enhanced knowledge of the molecular mechanisms controlling cardiac muscle contraction is crucial to the development of innovative diagnostic and pharmaceutical approaches to treat heart disease and other muscle conditions.

Selected publications:

  • Finley N.L. (2018) Revealing how an adenylate cyclase toxin uses bait and switch tactics in its activation. PLoS Biol. Feb 27;16(2):e2005356. doi: 10.1371/journal.pbio.2005356.
  • Springer, T.I., Johns, C.W., Cable, J.M., Lin, B.L., Sadayappan, S., Finley, N.L. (2017) Calcium-dependent interaction occurs between slow skeletal myosin binding protein C and calmodulin. Magnetochemistry, 4(1), 1;
  • Johns, C.W; Finley, N.L (2017) Site I Inactivation Impacts Calmodulin Calcium Binding and Activation of Bordetella pertussis Adenylate Cyclase Toxin. Toxins, 9, 389, doi:10.3390/toxins9120389.
  • Johns, C.W., Lee, A.B., Springer, T.I., Rosskopf, E.N, Hong, J.C., Turechek, W., Kokalis-Burelle, N., Finley, N.L. (2017) Using NMR-based metabolomics to monitor the biochemical composition of agricultural soils: A pilot study. Eur J Soil Biol, 83: 98-105.
  • Springer TI, Emerson CC, Johns CW, Finley NL. (2017) Interaction with adenylate cyclase toxin from Bordetella pertussis affects the metal binding properties of calmodulin. FEBS Open Bio. 2016 Dec 9;7(1):25-34.
  • Kuster D.W., Govindan S., Springer T.I., Martin J.L., Finley N.L., Sadayappan S. (2015) A hypertrophic cardiomyopathy-associated MYBPC3 mutation common in populations of South Asian descent causes contractile dysfunction. J. Biol. Chem. Jan 12
  • Springer T.I., Goebel E., Hariraju D., Finley N.L. (2014) Mutation in the β-hairpin of the Bordetella pertussis adenylate cyclase toxin modulates N-lobe conformation in calmodulin. Biochem Biophys Res Commun. Oct 10;453(1):43-8.
  • Finley N.L.,  Cuperman T.I. (2014). Cardiac Myosin Binding Protein C: A Structurally Dynamic Regulator of Myocardial Contractility. Pflügers Archiv. DOI 10.1007/s00424-014-1451-0. 
  • Sakthivel S., Finley N.L., Howarth J.W., Osinska H., Klevitsky R., Lorenz J.N., Rosevear P.R. and Robbins J. (2008)  Conserved Acidic-N’-region of Cardiac Troponin I is Critical in Regulating Myocardial Function. FASEB J. Apr;22(4):1246-57.
  • Sakthivel S., Finley N.L., Rosevear P.R., Lorenz J.N., Gulick J., Kim S., VanBuren P., Martin L.A., Robbins J. (2005) In vivo and in vitro analysis of cardiac troponin I phosphorylation J Biol. Chem. 280(1):703-14.
  • Finley, N.L. and Rosevear, P.R. (2004) Introduction of negative charge mimicking PKC phosphorylation of cardiac troponin I: Effects on cardiac troponin C. J. Biol. Chem. 279(52):54833-40.
  • Finley, N.L., Howarth, J. W. and Rosevear, P.R. (2004) Structure of the Mg2+ - Loaded C-Domain of Cardiac Troponin C Bound to the N-Domain of Cardiac Troponin I: Comparison with the Ca 2+ -Loaded Structure. Biochemistry, 43 (36), 11371-11379.
  • Finley, N.L., Howarth, J. W. and Rosevear, P.R. (2004) Structure of the Mg2+ - Loaded C-Domain of Cardiac Troponin C Bound to the N-Domain of Cardiac Troponin I: Comparison with the Ca2+ -Loaded Structure. Biochemistry, 43 (36), 11371-11379.