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


ABSTRACT: The Bam complex promotes the insertion of ?-barrel proteins into the bacterial outer membrane, but it is unclear whether it threads ?-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 ?-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 ?-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 ?-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.

SUBMITTER: Sikdar R 

PROVIDER: S-EPMC5670179 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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

Sikdar Rakesh R   Peterson Janine H JH   Anderson D Eric DE   Bernstein Harris D HD  

Nature communications 20171103 1


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  ...[more]

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