Biochemistry

Gerald Hazelbauer

Professor and Chair of Biochemistry

E-mail:hazelbauerg@missouri.edu

Office: 117 Schweitzer Hall

Mail: Biochemistry
117 Schweitzer Hall
University of Missouri
Columbia, MO 65211

Phone: 573-882-4845

Fax: 573-882-5635

Lab: 573-884-6334

Educational background

Notable honors and service

• Fellow, American Association for the Advancement of Science
• Fellow, American Academy of Microbiology
• FASEB Board of Directors 2004-2008
• Protein Society, Secretary/Treasurer 2005-2008; Council member 2008-2009
• Sloan Research Award in Neurosciences, 1973-75
• McKnight Neuroscience Development Award, 1982-85
• American Cancer Society Faculty Research Award, 1985-90
• Editorial Boards
  • Protein Science
  • The Journal of Microbiology
  • Journal of Bacteriology (1976-93)
• Conference Organization
  • Chair, Gordon Conference on Sensory Transduction in Microorganisms; Vice-Chair 1990, Chair 1992
  • Organizer, 24th Steenbock Symposium: Behavior and Signaling in Microorganisms, 1995

Research description

The aim of our research is to elucidate molecular mechanisms of transmembrane receptors and sensory transduction. For over 30 years our research group has provided important information about the transmembrane chemoreceptors and signaling complexes that mediate chemotaxis in Escherichia coli. We have helped make bacterial chemotaxis the best understood signaling system in biology and a favored subject for systems biology. Our experimental approaches combine biochemistry, biophysics and molecular genetics to investigate the "neurobiology" of bacteria.

We investigate processes by which receptors recognize ligand, signal across the membrane, produce intracellular signals, make supramolecular complexes, generate high sensitivity and wide dynamic range, integrate multiple signals, are covalently modified and mediate sensory adaptation. Elucidation of components and mechanisms involved in E. coli chemotaxis has wide impact because this sensory system is a paradigm for those systems that direct motility in the vast taxonomic range of microorganisms, many of which are biologically, medically and commercially important. In addition bacterial chemotaxis is one of the best understood members of the superfamily of "two-component" signaling systems. Such two-component systems contain histidine kinases and phosphorylated response regulators which mediate responses to many environmental signals. They occur across much of the diversity of living things, in most prokaryotes, plants and some single-celled eukaryotes.

Recent projects in the laboratory include structural probing of conformational changes in receptors residing unperturbed their natural cellular environment, characterization of receptor arrays in isolated membrane and investigation of the influence of supramolecular interactions on receptor function using the emerging technology of Nanodiscs to isolate a defined number of potentially interacting receptors. Our work often involves collaboration with leading laboratories in the application of biophysical, structural and modeling approaches to understanding complex biological systems. We will continue this multifaceted strategy of combining different approaches and disciplines. Members of our research group have the opportunity for training and experience in the entire range of these scientific areas.

Current areas of investigation include structural features of transmembrane receptors, cooperative interactions among chemoreceptors, the functional significance of supramolecular complexes, relating in vivo and in vitro activities of transmembrane receptors and manipulation of transmembrane proteins in native lipid bilayers.

Selected publications

Boldog, T. and Hazelbauer, G.L. 2004. Accessibility of introduced cysteines in chemoreceptor transmembrane helices reveals boundaries interior to bracketing charged residues. Protein Science 13, 1466-1475.

Li, M. and Hazelbauer, G.L. 2005. Adaptational assistance in clusters of bacterial chemoreceptors. Mol. Micro. 56, 1617-1626

Lai, W-C., Peach, M.L., Lybrand, T.P. and Hazelbauer, G.L. 2005. Diagnostic cross-linking of paired cysteine pairs demonstrates homologous structures for two chemoreceptor domains with low sequence identity. Protein Science 15, 94-101.

Lai, W.-C., Beel, B.D. and Hazelbauer G.L. 2006. Chemoreceptor adaptational modification reverses the piston movement of the transmembrane signaling helix. Mol. Micro. 61, 1081-1090.

Boldog, T., Grimme S., Li, M., Sligar S. G. and Hazelbauer, G.L. 2006. Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties. Proc. Natl. Acad. Sci. USA. 103, 11509-11514.

Lai, W.-C. and Hazelbauer, G.L. 2007. Analyzing Transmembrane Chemoreceptors using in vivo Disulfide Formation between Introduced Cysteines. Methods Enzy. 423, 299-316.

Boldog, T., Li, M. and Hazelbauer, G.L. 2007. Using Nanodiscs to Create Water-Soluble Transmembrane Chemoreceptors Inserted in Lipid Bilayers. Methods Enzy. 423, 317-335.

Hazelbauer, G.L., Falke, J.J., and Parkinson, J.S. 2008. Bacterial chemoreceptors: high-performance signaling in networked arrays. Trends Biochem. Sci. 33, 9-19.

Muppirala, U.K., Desensi, S., Lybrand, T.P., Hazelbauer, G.L. and Li, Z. 2009. Molecular Modeling of Flexible Arm-Mediated Interactions between Bacterial Chemoreceptors and their Modification Enzyme. Protein Science 18, 1702-1714

Employment opportunities

Postdoctoral opportunities

Research areas: Transmembrane receptors and sensory transduction in bacterial chemotaxis.

How to apply:

Electronic submission is encouraged, e-mail to biochemsearch@missouri.edu

Applicants should send CV and names of two references to:
Dr. Gerald Hazelbauer
Biochemistry
117 Schweitzer Hall
University of Missouri
Columbia, MO 65211