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Characterization of a stalled complex on the ?-barrel assembly machine.


ABSTRACT: The assembly of ?-barrel proteins into membranes is mediated by an evolutionarily conserved machine. This process is poorly understood because no stable partially folded barrel substrates have been characterized. Here, we slowed the folding of the Escherichia coli ?-barrel protein, LptD, with its lipoprotein plug, LptE. We identified a late-stage intermediate in which LptD is folded around LptE, and both components interact with the two essential ?-barrel assembly machine (Bam) components, BamA and BamD. We propose a model in which BamA and BamD act in concert to catalyze folding, with the final step in the process involving closure of the ends of the barrel with release from the Bam components. Because BamD and LptE are both soluble proteins, the simplest model consistent with these findings is that barrel folding by the Bam complex begins in the periplasm at the membrane interface.

SUBMITTER: Lee J 

PROVIDER: S-EPMC4978274 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature

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Characterization of a stalled complex on the β-barrel assembly machine.

Lee James J   Xue Mingyu M   Wzorek Joseph S JS   Wu Tao T   Grabowicz Marcin M   Gronenberg Luisa S LS   Sutterlin Holly A HA   Davis Rebecca M RM   Ruiz Natividad N   Silhavy Thomas J TJ   Kahne Daniel E DE  

Proceedings of the National Academy of Sciences of the United States of America 20160720 31


The assembly of β-barrel proteins into membranes is mediated by an evolutionarily conserved machine. This process is poorly understood because no stable partially folded barrel substrates have been characterized. Here, we slowed the folding of the Escherichia coli β-barrel protein, LptD, with its lipoprotein plug, LptE. We identified a late-stage intermediate in which LptD is folded around LptE, and both components interact with the two essential β-barrel assembly machine (Bam) components, BamA  ...[more]

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