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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.
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Anna Konovalova
Princeton University
Daniel Kahne
Harvard University
Thomas J. Silhavy
Merck & Co., Inc., Rahway, NJ, USA (United States)
Annual Review of Microbiology
Harvard University
Princeton University
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Konovalova et al. (Fri,) studied this question.
synapsesocial.com/papers/69d933759a6164e50fa3c333 — DOI: https://doi.org/10.1146/annurev-micro-090816-093754
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