Areas of Expertise
- Membrane Protein Assembly
- Ph.D. Washington State University
- Postdoc, University of California, Los Angeles
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.
- Yuan Y, Zweers JC, van Dijl JM & Dalbey RE. (2010), Protein transport across and into cell membranes in bacteria and archaea. Cell. Mol. Life Sci., 67, 179-199.
- Doğan Ekici Ö, Zhu J, Chung IY, Paetzel M, Dalbey RE & Pei D. (2009), Profiling the substrate specificity of viral protease VP4 by a FRET-based peptide Library Approach. Biochemistry, 48, 5753-5759.
- Doğan Ekici Ö, Paetzel M & Dalbey RE. (2008), Unconventional serine/threonine proteases: variations on the catalytic ser/his/asp triad configuration. Protein Science, 17, 2023-2037.
- Wang P, Shim E, Cravatt B, Jacobsen R, Schoeniger J, Kim AC, Paetzel M & Dalbey RE. (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.
- Xie K & Dalbey RE. (2008), Inserting proteins in bacterial membranes. Nature Reviews-Microbiology, 6, 234-244
- Xie K, Hessa T, Seppala S, Rapp M, von Heijne G & Dalbey RE. (2008), Features of transmembrane segments that promote the lateral release from the translocase into the lipid phase. Biochemistry, 46, 15153-15161.
- Celebi N & Dalbey RE. (2008). Mechanism and hydrophobic forces driving membrane protein insertion of cytochrome bo oxidase. J. Mol. Biol., 375, 1282- 1292.
- Yuan J, Phillips GJ & Dalbey RE. (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.
- Doğan Ekici Ö, Karla A, Paetzel M, Lively MO, Pei D & Dalbey RE. (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.
- Celebi N, Yi L, Facey SJ, Kuhn A & Dalbey RE. (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