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.
