Beta-barrel membrane proteins in Gram-negative bacteria, mitochondria, and chloroplasts are assembled by highly conserved multi-protein complexes.  The mechanism by which these molecular machines fold and insert their substrates is poorly understood.  Since the process has not been reproduced in a biochemical system, it has not been possible to dissect the folding and insertion pathway.  We have fully purified the components that fold and insert E. coli outer membrane proteins, and we have reconstituted beta-barrel protein assembly in proteoliposomes using the enzymatic activity of a protein substrate to report on its folding state.  We demonstrate that the assembly of this protein occurs without an energy source but requires a soluble chaperone in addition to the multi-protein assembly complex.

Reconstitution of outer membrane protein assembly from purified components

244th National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.