Abstract
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. βα-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 αÎ ±-helical membrane protein assembly will reveal whether there are general principles that guide the folding and insertion of all membrane proteins.
Original language | English (US) |
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Pages (from-to) | 189-210 |
Number of pages | 22 |
Journal | Annual review of biochemistry |
Volume | 80 |
DOIs | |
State | Published - Jul 7 2011 |
All Science Journal Classification (ASJC) codes
- Biochemistry
Keywords
- Bam complex
- POTRA domain
- chaperone
- outer membrane protein
- protein folding
- β-strand augmentation