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Methods Mol Biol. 2015;1329:1-16. doi: 10.1007/978-1-4939-2871-2_1.

The β-Barrel Assembly Machinery Complex.

Author information

1
Research School of Biology, Australian National University, Canberra, ACT, 0200, Australia. denisse.leyton@anu.edu.au.
2
Department of Microbiology, Monash University, Building 77, 23 Innovation Walk, Clayton Campus, Melbourne, VIC, 3800, Australia.
3
Department of Microbiology, Monash University, Building 77, 23 Innovation Walk, Clayton Campus, Melbourne, VIC, 3800, Australia. trevor.lithgow@monash.edu.

Abstract

The outer membranes of gram-negative bacteria contain integral membrane proteins, most of which are of β-barrel structure, and critical for bacterial survival. These β-barrel proteins rely on the β-barrel assembly machinery (BAM) complex for their integration into the outer membrane as folded species. The central and essential subunit of the BAM complex, BamA, is a β-barrel protein conserved in all gram-negative bacteria and also found in eukaryotic organelles derived from bacterial endosymbionts. In Escherichia coli, BamA docks with four peripheral lipoproteins, BamB, BamC, BamD and BamE, partner subunits that add to the function of the BAM complex in outer membrane protein biogenesis. By way of introduction to this volume, we provide an overview of the work that has illuminated the mechanism by which the BAM complex drives β-barrel assembly. The protocols and methodologies associated with these studies as well as the challenges encountered and their elegant solutions are discussed in subsequent chapters.

KEYWORDS:

BamA; Omp85; Outer membrane; Outer membrane β-barrel proteins (OMPs); Periplasmic chaperones; β-barrel; β-barrel assembly machinery (BAM)

PMID:
26427672
DOI:
10.1007/978-1-4939-2871-2_1
[Indexed for MEDLINE]

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