Perry F. Churchill

Associate Professor

Phone: (205) 348-4097

Email: pchurchi@biology.as.ua.edu

Perry Churchill received a Ph.D. in Chemistry from Wayne State University in 1979. He was appointed Assistant Professor at the University of Alabama in 1986. Dr. Churchill has served as Associate Professor at the University of Alabama since 1992.

Research Interests

My research interests utilize biochemistry and molecular biology to study the structure and function of proteins. Proteins currently being studied are involved in diverse functions and are derived from a wide variety of organisms. From bacteria the genes encoding enzymes involved in the oxidation of polycyclic aromatic hydrocarbons (PAH’s) have been cloned and numerous proteins expressed and purified. Additionally, proteins involved in the regulation of the expression of these biodegradation genes have also been expressed and purified. Results of such studies will lead to a better understanding of the bioremediation of PAH’s.

The incorrect folding of cellular proteins in all organisms can occur in response to a number of stresses such as heat shock and free radical damage. The folding of proteins into their correct three dimensional native conformations often requires the assistance of other proteins known as molecular chaperones. The structure and function of proteins that serve as chaperones has been investigated using purified proteins derived from the expression of their genes in bacteria.

A protein kinase from the plant model organism Arabidopsis thaliana that is involved in the detection of fungal pathogens has been cloned, expressed, and purified. We are utilizing this protein to elucidate the signaling pathway used by this plant to defend itself against pathogen attach. We are also interested in the role played by an increase in expression of the genes encoding molecular chaperones following pathogen contact.


Selected Publications

Burdette A.J., Churchill P.F., Caldwell,G.A., and Caldwell K.A. 2010. The early-onset torsin dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro. Cell Stress and Chaperones. 15:605-617.

Wakefield, W.S., M.J. Powell,P. M. Letcher, D.J.S. Barr, P.F.Churchill, J.E. Longcore, and S.F. Chen. 2010. A molecular phylogenetic evaluation of Spizellomycetales. Mycologia 102: 596-604.

Churchill,Perry F., Morgan, Adam C. and Kitchens, Elizabeth 2008. Characterization of a pyrene-degrading Mycobacterium sp. Strain CH-2. Journal of Environmental Science and Health. 43:698-706.

Faircloth, Lindsay M., Churchill, Perry F., Caldwell, Guy A.,and Caldwell,Kim A.2008. The microtubule-associated protein, NUD-1, exhibits chaperone activity in vitro. Cell Stress and Chaperones. 14:95-103.

Weber, Karrie A., Urrutia, Matilde, M.,Churchill,Perry, F.,Kukkadapu, Ravi,K., and Roden,Eric E. 2006. Anaerobic redox cycling of iron by freshwater sediment microorganisms. Environmental Microbiology.8:100-113.

Harper, Jennifer Paige, Churchill,Perry F.,Lokey-Flippo, Laura, and Lalor, Melinda M 2005. Effect of Mycobacterium Sp. Strain CH1 and Mycobacterium Sp. Strain CH2 on the degradation of Four-Ring Creosote Compounds. Journal of Environmental Science and Health. 40:493-507.