Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 113, Issue 31, Pages 8717-8722Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1604100113
Keywords
outer membrane; Bam complex; beta-barrel; protein folding
Categories
Funding
- National Institutes of Health Awards [F31GM116210, F32GM108258, GM34821, GM100951, AI081059]
- National Science Foundation Graduate Research Fellowship Program Award [DGE1148900]
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The assembly of beta-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 beta-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 beta-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.
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