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Annu Rev Microbiol. 2017 Sep 8;71:539-556. doi: 10.1146/annurev-micro-090816-093754.

Outer Membrane Biogenesis.

Author information

1
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544; email: tsilhavy@princeton.edu.
2
Department of Chemistry and Chemical Biology and.
3
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138.
4
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.

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.

KEYWORDS:

LptD; envelope biogenesis; lateral gate; outer membrane protein; protein folding

[Indexed for MEDLINE]
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