Chemistry Faculty:
Jeffrey L. Urbauer, Ph.D.
Associate Professor
Phone: 706-542-7922
E-mail: urbauer@chem.uga.edu
Biographical Information
Ph.D., University of Nebraska, 1987
NIH Postdoctoral Fellow, University of Wisconsin, 1988-1992
Research Interests
- Protein structure and function
- NMR spectroscopy of proteins and protein complexes
- Biophysical characterization of proteins
- Structural biology
The molecular details that define the structure, stability and function of interesting proteins and protein complexes, and those that dictate how proteins fold and interact with one another, are the focus of the research in the Urbauer laboratory. We employ an approach combining modern biophysical and molecular biology techniques. Advanced biomolecular NMR spectroscopy is emphasized, and is used to analyze the structures of proteins at high resolution and to study their dynamics and stabilities. For example, we have used NMR to solve the structure of a dimeric regulator of prokaryotic transcription regulation, and are currently using site-directed mutagenesis along with analytical ultracentrifugation, fluorescence spectroscopy, and other biophysical measurements to characterize comprehensively the contributions of individual amino acids to the stability and reactivity of the protein. Our core projects include the study of gene regulation and novel regulators of transcription initiation in bacteria, calcium signaling mediated by the quintessential and ubiquitous calcium signaling protein calmodulin, and regulation of alginate biosynthesis and pathogenesis in Pseudomonas aeruginosa . These projects are important fundamentally, and they are relevant for biomedical concerns including antibiotic target development, oxidative stress and biological aging, and diseases such as cystic fibrosis.
Publications
Slaughter, B. D., Urbauer, R. J., Urbauer, J. L. and Johnson, C. K. (2007) Mechanism of calmodulin recognition of the binding domain of isoform 1b of the plasma membrane Ca2+-ATPase: Kinetic pathway and effects of methionine oxidation. Biochemistry 46, 4045-4054.
Cowley, A. B., Bieber Urbauer, R. J., and Urbauer, J. L. (2005) 1H, 13C and 15N NMR assignments for AlgH, a putative transcriptional regulator from Pseudomonas aeruginosa. J. Biomol. NMR 33, 74.
Anbanandam, A., Bieber Urbauer, R. J., Bartlett, R. J., Smallwood, H. S., Squier, T. C., and Urbauer, J. L. (2005) Mediating molecular recognition by methionine oxidation: Conformational switching by oxidation of methionine in the carboxyl-terminal domain of calmodulin. Biochemistry 44, 9486-9496.
Yang, W., Wilkins, A. L., Ye, Y., Liu, Z.-R., Urbauer, J. L., Hellinga, H. W., Kearney, A. van der Merwe, P. A., and Yang, J. J. (2005) Design of a calcium-binding protein with desired structure and cell adhesion function. J. Am. Chem. Soc. 127, 2085-2093.
Bieber Urbauer, R. J., Rosasco, S. E., Gilmore, J. M., Hattle, J. M., Cowley, A. B. and Urbauer, J. L. (2005) Cloning and high-yield overexpression and purification of AlgH, a regulator of alginate biosynthesis in Pseudomonas aeruginosa. Prot. Expr. Purif. 43, 57-64.
Gregory, B., Nickels, B. E., Garrity, S., Severinova, E., Minakhin, L., Bieber Urbauer, R. J., Urbauer, J. L., Heyduk, T., Severinov, K., and Hochschild, A. (2004) A regulator that inhibits transcription by targeting an intersubunit interaction of the RNA polymerase holoenzyme. Proc. Natl. Acad. Sci. U.S.A. 101, 4554-4559.
Osborn, K., Bartlett, R. K., Bieber Urbauer, R. J., Urbauer, J. L., and Johnson, C. K. (2004) Single-molecule dynamics reveal an altered conformation for the autoinhibitor domain of plasma-membrane Ca2+-ATPase bound to oxidatively modified calmodulin. Biochemistry 43, 12937-12944.
Allen, M. W., Bieber Urbauer, R. J., Zaidi, A., Williams, T. D., Urbauer, J. L., and Johnson, C. K. (2004) Fluroescence Labeling, Purification, and Immobilization of a Double Cysteine Mutant Calmodulin Fusion Protein for Single-Molecule Experiments. Anal. Biochem. 325, 273-284.
Zheng, K., Makagiansar, I. T., Wang, M., Urbauer, J. L., Kuczera, K., and Siahaan, T. J. (2004) Expression, purification and structural study of the EC4 domain of E-cadherin. Protein Expr. and Purif. 33, 72-79.