The β-barrel assembly machinery complex

Denisse L. Leyton, Matthew J. Belousoff, Trevor Lithgow

    Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

    9 Citations (Scopus)

    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 a ssembly m achinery (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.

    Original languageEnglish
    Title of host publicationMethods in Molecular Biology
    PublisherHumana Press Inc.
    DOIs
    Publication statusPublished - 1 Apr 2015

    Publication series

    NameMethods in Molecular Biology
    Volume1329
    ISSN (Print)1064-3745

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