TY - JOUR
T1 - Characterization of a stalled complex on the β-barrel assembly machine
AU - Lee, James
AU - Xue, Mingyu
AU - Wzorek, Joseph S.
AU - Wu, Tao
AU - Grabowicz, Marcin
AU - Gronenberg, Luisa S.
AU - Sutterlin, Holly A.
AU - Davis, Rebecca M.
AU - Ruiz, Natividad
AU - Silhavy, Thomas J.
AU - Kahne, Daniel E.
N1 - Funding Information:
This work was supported by funds from the National Institutes of Health Awards F31GM116210 (to J.L.), F32GM108258 (to J.S.W.), GM34821 (to T.J.S.), GM100951 (to N.R.), and AI081059
PY - 2016/8/2
Y1 - 2016/8/2
N2 - 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.
AB - 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.
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U2 - 10.1073/pnas.1604100113
DO - 10.1073/pnas.1604100113
M3 - Article
C2 - 27439868
AN - SCOPUS:84982698581
SN - 0027-8424
VL - 113
SP - 8717
EP - 8722
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 31
ER -