β-Barrel membrane protein assembly by the Bam complex.

Christine L Hagan, Thomas J Silhavy, Daniel Kahne

Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA. clhagan@fas.harvard.edu

Annual review of biochemistry 2011

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β-barrel membrane proteins perform important functions in the outer membranes (OMs) of Gram-negative bacteria and of the mitochondria and chloroplasts of eukaryotes. The protein complexes that assemble these proteins in their respective membranes have been identified and shown to contain a component that has been conserved from bacteria to humans. β-barrel proteins are handled differently from α-helical membrane proteins in the cell in order to efficiently transport them to their final locations in unfolded but folding-competent states. The mechanism by which the assembly complex then binds, folds, and inserts β-barrels into the membrane is not well understood, but recent structural, biochemical, and genetic studies have begun to elucidate elements of how the complex provides a facilitated pathway for β-barrel assembly. Ultimately, studies of the mechanism of β-barrel assembly and comparison to the better-understood process of α-helical membrane protein assembly will reveal whether there are general principles that guide the folding and insertion of all membrane proteins.

Citation

Christine L Hagan, Thomas J Silhavy, Daniel Kahne. β-Barrel membrane protein assembly by the Bam complex. Annual review of biochemistry. 2011;80:189-210