Folding of a bacterial integral outer membrane protein is initiated in the periplasm

Rakesh Sikdar, Janine H. Peterson, D. Eric Anderson and Harris D. Bernstein ()
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Rakesh Sikdar: National Institutes of Health
Janine H. Peterson: National Institutes of Health
D. Eric Anderson: National Institutes of Health
Harris D. Bernstein: National Institutes of Health

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: Abstract The Bam complex promotes the insertion of β-barrel proteins into the bacterial outer membrane, but it is unclear whether it threads β-strands into the lipid bilayer in a stepwise fashion or catalyzes the insertion of pre-folded substrates. Here, to distinguish between these two possibilities, we analyze the biogenesis of UpaG, a trimeric autotransporter adhesin (TAA). TAAs consist of three identical subunits that together form a single β-barrel domain and an extracellular coiled-coil (“passenger”) domain. Using site-specific photocrosslinking to obtain spatial and temporal insights into UpaG assembly, we show that UpaG β-barrel segments fold into a trimeric structure in the periplasm that persists until the termination of passenger-domain translocation. In addition to obtaining evidence that at least some β-barrel proteins begin to fold before they interact with the Bam complex, we identify several discrete steps in the assembly of a poorly characterized class of virulence factors.

Date: 2017
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DOI: 10.1038/s41467-017-01246-4

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