Melinda Faulkner

Melinda Faulkner

Department Chair and Associate Professor

    Olin Hall 101A
    (309) 677-3019
   mfaulkner@bradley.edu

 

Ph.D., Microbiology and Molecular Genetics, Harvard Medical School
B.S., Microbiology, University of Illinois at Urbana-Champaign

Biography

Dr. Faulkner studies how bacterial cells protect themselves against stressful conditions, in particular oxidative stress. Organisms that live in the presence of oxygen (including humans!) generate toxic oxygen-containing molecules such as hydrogen peroxide. Furthermore, our immune systems produce similar toxic oxygen species to combat bacterial infections. These reactive oxygen molecules damage enzymes and membranes, and may cause mutation or even cell death. Thus, the ability of cells, both microbial and human, to sense these damaging molecules and respond to them with an appropriate antioxidant defense is vital for their survival. In the laboratory, we are using molecular genetic techniques to investigate the enzymes and regulatory mechanisms used by bacteria to survive under conditions of oxidative stress.

 

Teaching

BIO 101 Life Sciences I; BIO 151 Molecules to Cells; BIO 301 Biotechnology and Society; BIO 406 General Microbiology; BIO 506 Advanced Microbiology

 

Scholarship

  • Zwick JV, Noble S, Ellaicy YK, Coe GD, Hakey DJ, King AN, Sadauskas AJ, and Faulkner MJ. 2017. AhpA is a peroxidase expressed during biofilm formation. MicrobiologyOpen 6: e00403.
  • Broden NJ, Flury S, King AN, Schroeder BW, Coe GD, and Faulkner MJ. 2016. Insights into the function of a second, non-classical Ahp peroxidase, AhpA, in oxidative stress resistance in Bacillus subtilis. Journal of Bacteriology 198 (7): 1044-1057.
  • Ma Z, Faulkner MJ, and Helmann JD. 2012. Origins of specificity and cross-talk in metal ion sensing by Bacillus subtilis Fur. Molecular Microbiology 86(5): 1144-1155. 
  • Lobstein J, Emrich C, Jeans C, Faulkner M, Riggs P, and Berkmen M. 2012. Shuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm. Microbial Cell Factories 11: 56. 
  • Faulkner MJ, Ma Z, Fuangthong M, Helmann JD. 2012. Derepression of the Bacillus subtilis PerR peroxide stress response leads to iron deficiency. Journal of Bacteriology 194: 1226-35. 
  • Feeney MA, Veeravalli K, Boyd D, Gon S, Faulkner MJ, Georgiou G, and Beckwith J. 2011. Repurposing lipoic acid changes electron flow in two important metabolic pathways of Escherichia coli. Proceedings of the National Academy of Sciences of the USA 108: 7991-7996. 
  • Faulkner MJ and Helmann JD. 2011. Peroxide stress elicits adaptive changes in bacterial metal ion homeostasis. Antioxidants and Redox Signaling 15:175-189 (Review) 
  • Faulkner MJ, Veeravalli K, Gon S, Georgiou G, and Beckwith J.  2008. Functional plasticity of a peroxidase allows evolution of diverse disulfide reducing pathways. Proceedings of the National Academy of Sciences of the USA 105: 6735-6740. 
  • Yamamoto Y, Ritz D, Planson AG, Jonsson TJ, Faulkner MJ, Boyd D, Beckwith J, and Poole LB.  2008.  Mutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activity. Molecular Cell 29: 36-45. 
  • Gon S, Faulkner MJ, and Beckwith J.  2006. In vivo requirement for glutaredoxins and thioredoxins in the reduction of the ribonucleotide reductases of E. coli. Antioxidants and Redox Signaling 8: 735-742.

 

 

Licensures and Certifications

Biological Patent

  • Beckwith J, Ritz D, Faulkner M, Gon S, and Georgiou G. Prokaryotic host cells for expressing proteins rich in disulfide bonds. US2007/67306. 8 November 2007.