Abstract
The hallmark of gram-negative bacteria and organelles such as mitochondria and chloroplasts is the presence of an outer membrane. In bacteria such as Escherichia coli, the outer membrane is a unique asymmetric lipid bilayer with lipopolysaccharide in the outer leaflet. Integral transmembrane proteins assume a β-barrel structure, and their assembly is catalyzed by the heteropentameric Bam complex containing the outer membrane protein BamA and four lipoproteins, BamB-E. How the Bam complex assembles a great diversity of outer membrane proteins into a membrane without an obvious energy source is a particularly challenging problem, because folding intermediates are predicted to be unstable in either an aqueous or a hydrophobic environment. Two models have been put forward: the budding model, based largely on structural data, and the BamA assisted model, based on genetic and biochemical studies. Here we offer a critical discussion of the pros and cons of each.
Original language | English (US) |
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Pages (from-to) | 539-556 |
Number of pages | 18 |
Journal | Annual Review of Microbiology |
Volume | 71 |
DOIs | |
State | Published - Sep 8 2017 |
All Science Journal Classification (ASJC) codes
- Microbiology
Keywords
- Envelope biogenesis
- Lateral gate
- LptD
- Outer membrane protein
- Protein folding