Faculty and Staff

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

  • PHD, University of Alabama at Birmingham (2013)
  • MS, University of Alabama at Birmingham (2011)
  • BS, University of Alabama at Birmingham (2008)

Areas of Expertise

Biochemistry, Enzymology

Publications

Recent Peer-Reviewed Publications:

1. J.M. Miller, C.A. Brambley, and J.D. Marsee. “Examination of the Role of Mg2+ in the Mechanism of Nucleotide Binding to the Monomeric YME1L AAA+ Domain.” ACS Biochemistry. (2020). In Press.

2. C.A. Brambley, A.L. Bolay, H. Salvo, A.L. Jansch, T.J. Yared, J.M. Miller, J.R. ...

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Recent Peer-Reviewed Publications:

1. J.M. Miller, C.A. Brambley, and J.D. Marsee. “Examination of the Role of Mg2+ in the Mechanism of Nucleotide Binding to the Monomeric YME1L AAA+ Domain.” ACS Biochemistry. (2020). In Press.

2. C.A. Brambley, A.L. Bolay, H. Salvo, A.L. Jansch, T.J. Yared, J.M. Miller, J.R. Wallen, and M.H. Weiland. “Structural Characterization of Sphingomonas sp. KT-1 PahZ1 Catalyzed Biodegradation of Thermally Synthesized poly(aspartic acid).” ACS Sustainable Chem. Eng. 8(29), 10702-10713. (2020).

3. S. Moore, A. Pickens, J. Rodriguez, J.D. Marsee, and J.M. Miller. “Fluorescence Methods Applied to the Description of Urea-Dependent YME1L Protease Unfolding.” Biomolecules, 10(4), 656. (2020).

4. C.A. Brambley, J.D. Marsee, N. Halper, and J.M. Miller. "Characterization of Mitochondrial YME1L Protease Oxidative Stress Induced Conformational State." J. Mol. Biol. 431(6):1250-1266. (2019).

5. J.D. Marsee, A. Ridings, T. Yu, and J.M. Miller. “Mycobacterium tuberculosis ClpC1 N- terminal Domain is Dispensable for Adaptor Protein-Dependent Allosteric Regulation.” Int. J. Mol. Sci. 19(11), 3651. (2018).

6. J. M. Miller, H. Chaudhary, and J.D. Marsee. "Phylogenetic analysis predicts structural divergence for proteobacterial ClpC proteins." J Struct Biol 201(1): 52-62. (2018).

(† Indicates undergraduate students)

Book Chapters:

1. J.M. Miller and C. Brambley. “Enzyme Active Site Architecture: The Whole is Greater than the Sum of the Parts.” ACS Symposium Series (Bridging Structure and Function in Mechanistic Enzymology). American Chemical Society. 2020. 

2. J.M. Miller. “Introduction: Viewing Science through Multiple Lenses.” ACS Symposium Series (Bridging Structure and Function in Mechanistic Enzymology). American Chemical Society. 2020. 

A complete listing of Dr. Miller's peer-reviewed publications can be found at:

Justin M. Miller Google Scholar

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Research / Scholarly Activity

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...

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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. 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 manipulate normal proteolytic function.

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Courses

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