Dr. Dalbey received his B.S. degree in chemistry from University of Washington in 1978 and his Ph.D. in Biochemistry from Washington State University in 1983. That same year he joined the laboratory of Professor William Wickner at UCLA as a NIH postdoctoral fellow. Then he moved from the West coast to the Midwest to become a member of the faculty at The Ohio State University in 1987. He was promoted to Full Professor in 1999. Professor Dalbey won a Junior Faculty Award (1989-1992) from the American Cancer Society. In 1996, he was a visiting professor at the Federal Institute of Technology in Lausanne, Switzerland working with Professor Horst Vogel. Dr. Dalbey is a member of the American Chemical Society, Federation of American Societies for Experimental Biology, Sigma Xi, American Society of Microbiology, and the honor Society of Phi Kappa Phi. He is an elected fellow of the AAAS.
Our lab’s central interest is the determination of how proteins are transported and inserted into membrane to obtain their proper structure. We are employing biochemical and in vivo approaches to understand membrane protein assembly. We have identified a novel protein, YidC that specializes in membrane protein topogenesis. The general relevance of this finding is underscored by the homology of YidC to the mitochondrial Oxa1, which functions in a novel pathway for insertion of inner membrane proteins from the mitochondrial matrix compartment. The goal now is to determine the substrate specificity of YidC, to determine the function of YidC in the integration and folding of multispanning membrane proteins, define the structural features of YidC and the insertion pore of the YidC dimer. Another serious interest here is the study of proteases involved in the cleavage of proteins and peptides that are transiently associated with cellular membranes. These proteases such as signal peptidase and signal peptide peptidases are crucially important for a wide range of essential biological processes. We are very interested in how the cell meets the “chemical challenge” of peptide bond hydrolysis in proteins that are shielded by non-aqueous environments.
Recent graduates from the Dalbey lab hold faculty positions at the University of Pittsburg, Simon Fraser University, and Kwandong University. They hold research positions at National Institutes of Health (NIH), MIT, and Duke, and have industrial positions at Novartis, Eli Lilly, and Abbott Pharmaceuticals. Funding from the lab has come primarily from NIH and National Science Foundation (NSF) over the years.
Ross Dalbey will be taking graduate students in the Fall of 2010. More detailed information can be found at http://dalbey.group.chemistry.ohio-state.edu.
Celebi, N., Yi, L., Facey, S. J., Kuhn, A. and Dalbey, R. E. (2006), Membrane protein biogenesis of subunit II of cytochrome bo oxidase: contrasting requirements for the insertion of N-terminal and C-terminal domains. J. Mol. Biol., 357, 1428-1436
Doğan Ekici, Ö., Karla, A., Paetzel, M., Lively, M. O., Pei, D. and Dalbey, R. E. (2007), Altered -3 substrate specificity of E. coli signal peptidase I mutants as revealed by screening a combinatorial peptide library. J. Biol. Chem., 282, 417-425.
Yuan, J., Phillips, G. J. and Dalbey, R. E. (2007), Isolation of cold sensitive yidC mutants provide insights into the substrate Profile of the YidC insertase and the Importance of transmembrane three in YidC function. J. Bacteriol, 189, 8961-8972.
Celebi, N. and Dalbey, R. E. (2008). Mechanism and hydrophobic forces driving membrane protein insertion of cytochrome bo oxidase. J. Mol. Biol., 375, 1282- 1292.
Xie, K., Hessa, T., Seppala, S., Rapp, M., von Heijne, G. and Dalbey, R. E. (2008), Features of transmembrane segments that promote the lateral release from the translocase into the lipid phase. Biochemistry, 46, 15153-15161.
Xie, K. and Dalbey, R. E. (2008), Inserting proteins in bacterial membranes. Nature Reviews-Microbiology, 6, 234-244
Wang, P., Shim, E., Cravatt, B., Jacobsen, R., Schoeniger, J., Kim, AC., Paetzel., M. and Dalbey, R. E. (2008), Escherichia coli signal peptide peptidase A is a serine-lysine protease with a lysine recruited to the nonconserved amino-terminal domain in the S49 protease family. Biochemistry, 47, 6361-6369.
Doğan Ekici, Ö., Paetzel, M. and Dalbey, R. E. (2008), Unconventional serine/threonine proteases: variations on the catalytic ser/his/asp triad configuration. Protein Science, 17, 2023-2037.
Doğan Ekici, Ö, Zhu, J., Chung, IY, Paetzel, M., Dalbey, R. E., and Pei, D. (2009), Profiling the substrate specificity of viral protease VP4 by a FRET-based peptide Library Approach. Biochemistry, 48, 5753-5759.
Yuan, Y., Zweers, J. C. Zweers, van Dijl, J. M. and Dalbey, R. E. (2010), Protein transport across and into cell membranes in bacteria and archaea. Cell. Mol. Life Sci., 67, 179-199.