Outer Membrane Biogenesis

被引:203
|
作者
Konovalova, Anna [1 ]
Kahne, Daniel E. [2 ,3 ,4 ]
Silhavy, Thomas J. [1 ]
机构
[1] Princeton Univ, Dept Mol Biol, Princeton, NJ 08544 USA
[2] Harvard Univ, Dept Chem & Chem Biol, Cambridge, MA 02138 USA
[3] Harvard Univ, Dept Cellular & Mol Biol, Cambridge, MA 02138 USA
[4] Harvard Med Sch, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA
来源
关键词
envelope biogenesis; outer membrane protein; LptD; lateral gate; protein folding; BARREL ASSEMBLY MACHINERY; ESCHERICHIA-COLI BAMB; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; PERIPLASMIC DOMAIN; LIPID-BILAYERS; PROTEIN-A; ESSENTIAL COMPONENT; SERINE-PROTEASE; COMPLEX;
D O I
10.1146/annurev-micro-090816-093754
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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 beta-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.
引用
收藏
页码:539 / 556
页数:18
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