Dr. Justin M. Miller

Assistant Professor

Dr. Justin M. Miller
615-494-7917
Room 3141, Science Building (SCI)
MTSU Box 68, Murfreesboro, TN 37132

Degree Information

  • Ph.D., University of Alabama at Birmingham (2013)
  • M.S., University of Alabama at Birmingham (2011)
  • B.S., University of Alabama at Birmingham (2008)

Areas of Expertise

Biochemistry, Enzymology

Biography

  All organisms require a class of cellular machinery termed ATP-dependent proteases that are responsible for the highly regulated removal of misfolded or properly folded proteins in cellular quality control pathways. These machines are conceptually similar to paper shredders, where material is fed into an interior compartment and shredded. On the molecular level, ATP-dependent proteases are responsible for recognizing specific proteins or polypeptides and “shredding” them th...

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  All organisms require a class of cellular machinery termed ATP-dependent proteases that are responsible for the highly regulated removal of misfolded or properly folded proteins in cellular quality control pathways. These machines are conceptually similar to paper shredders, where material is fed into an interior compartment and shredded. On the molecular level, ATP-dependent proteases are responsible for recognizing specific proteins or polypeptides and “shredding” them through a process called proteolysis. In bacteria, ATP-dependent proteases are assembled from two components that include an adenosine triphosphate (ATP)-fueled motor and an associated protease that catalyzes protein/polypeptide degradation. In the assembled ATP-dependent protease complex, the motor component uses the energy of ATP hydrolysis to thread polypeptide substrates into the protease for degradation. Due to their vital role in maintaining cellular health, inhibition of any component of the ATP-dependent protease complex may serve as a viable route to the development of novel therapeutics to infections caused by pathogenic bacteria.
       Research in the Miller laboratory focuses on furthering our understanding of ATP-dependent proteases from pathogenic bacteria. We combine physical biochemistry methods such as fluorescence spectroscopy, pre-steady state kinetics, coupled-enzyme assays, etc. with other disciplines that include organic chemistry and evolutionary biology with the goal of understanding how motor proteins recognize and translocate protein substrates into the associated protease for degradation. This knowledge is important because it will advance our mission towards the development of drug molecules designed to interfere with normal proteolytic function. A central philosophy of the Miller lab is that if we can understand how these proteins function, we can then devise novel approaches to disrupting their function in pathogenic bacteria.

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Publications

  • Justin M. Miller, Hamza Chaudhary, and Justin D. Marsee. “Phylogenetic Analysis Predicts Structural Divergence for Proteobacterial ClpC Proteins.” Journal of Structural Biology, 201(1):52-62. (2018).
  • J. M.  Miller and E. J. Enemark. "Fundamental Characteristics of AAA+ Protein Family Structure and Function." Archaea. (2016).
  • J. M.  Miller and E. J. Enemark. "Archaeal MCM Prote...
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  • Justin M. Miller, Hamza Chaudhary, and Justin D. Marsee. “Phylogenetic Analysis Predicts Structural Divergence for Proteobacterial ClpC Proteins.” Journal of Structural Biology, 201(1):52-62. (2018).
  • J. M.  Miller and E. J. Enemark. "Fundamental Characteristics of AAA+ Protein Family Structure and Function." Archaea. (2016).
  • J. M.  Miller and E. J. Enemark. "Archaeal MCM Proteins as an Analog for the Eukaryotic Mcm2-7 Helicase to Reveal Essential Features of Structure and Function." Archaea, 14. (2015).
  • T. Li, C.L. Weaver, J. Lin, E.C. Duran, J. M. Miller and A. L. Lucius. "Escherichia coli ClpB is a non-processive polypeptide translocase." Biochem J, 470(1): 39-52. (2015).
  • J. M. Miller, B. T. Arachea, L. B. Epling and E. J. Enemark. “Analysis of the crystal structure of an active MCM hexamer.” eLife, 3. (2014).
  • J. M. Miller and A. L. Lucius. “Dependence of ClpA Catalyzed Polypeptide Translocation on ATPgS.” Biophys. Chem. 185, 58-69. (2014).
  • J. M. Miller, J. Lin, T. Li, and A. L. Lucius. “E.coli ClpA catalyzed polypeptide translocation is allosterically controlled by the protease ClpP.” J. Mol. Biol.  425 (15), 2795-812. (2013).
  • A. L. Lucius, J. M. Miller & B. Rajendar. “Application of the Sequential n-Step Kinetic Mechanism to Polypeptide Translocases.” Methods Enzymol 488, 239-64. (2011).

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Courses

CHEM4500 (Biochemistry 1), CHEM4510 (Biochemistry 2), CHEM4520 (Topics in Biochemistry), CHEM4530 (Biochemical Techniques)