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

James Lee, Mingyu Xue, Joseph S. Wzorek, Tao Wu, Marcin Grabowicz, Luisa S. Gronenberg, Holly A. Sutterlin, Rebecca M. Davis, Natividad Ruiz, Thomas J. Silhavy, Daniel E. Kahne

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Abstract

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 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.

Original languageEnglish (US)
Pages (from-to)8717-8722
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume113
Issue number31
DOIs
StatePublished - Aug 2 2016

All Science Journal Classification (ASJC) codes

  • General

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    Lee, J., Xue, M., Wzorek, J. S., Wu, T., Grabowicz, M., Gronenberg, L. S., Sutterlin, H. A., Davis, R. M., Ruiz, N., Silhavy, T. J., & Kahne, D. E. (2016). Characterization of a stalled complex on the β-barrel assembly machine. Proceedings of the National Academy of Sciences of the United States of America, 113(31), 8717-8722. https://doi.org/10.1073/pnas.1604100113