Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA β-barrel

Matthew T. Doyle and Harris D. Bernstein ()
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Matthew T. Doyle: National Institutes of Health
Harris D. Bernstein: National Institutes of Health

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: Abstract The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). The central BAM subunit (BamA) itself contains a β-barrel domain that is essential for OM protein biogenesis, but its mechanism of action is unknown. To elucidate its function, here we develop a method to trap a native Escherichia coli β-barrel protein bound stably to BamA at a late stage of assembly in vivo. Using disulfide-bond crosslinking, we find that the first β-strand of a laterally ‘open’ form of the BamA β-barrel forms a rigid interface with the C-terminal β-strand of the substrate. In contrast, the lipid-facing surface of the last two BamA β-strands forms weaker, conformationally heterogeneous interactions with the first β-strand of the substrate that likely represent intermediate assembly states. Based on our results, we propose that BamA promotes the membrane integration of partially folded β-barrels by a ‘swing’ mechanism.

Date: 2019
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DOI: 10.1038/s41467-019-11230-9

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