β-barrel membrane protein assembly by the bam complex

Christine L. Hagan, Thomas J. Silhavy, Daniel Kahne

Research output: Contribution to journalArticle

218 Scopus citations

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 languageEnglish (US)
Pages (from-to)189-210
Number of pages22
JournalAnnual review of biochemistry
Volume80
DOIs
StatePublished - Jul 7 2011

All Science Journal Classification (ASJC) codes

  • Biochemistry

Keywords

  • Bam complex
  • POTRA domain
  • chaperone
  • outer membrane protein
  • protein folding
  • β-strand augmentation

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