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• W1994121837 endingPage "5156" @default.
• W1994121837 startingPage "5151" @default.
• W1994121837 abstract "In Gram-negative bacteria, integral outer membrane β-barrel proteins (OMPs) are assembled by the beta-barrel assembly machine (Bam) complex. The essential components of this complex are the OMP BamA [which contains a carboxyl-terminal β-barrel and an amino-terminal periplasmic module composed of five polypeptide transport associated (POTRA) domains] and the lipoprotein BamD. In Escherichia coli , the Bam complex also contains three nonessential lipoproteins (BamBCE), all of which require the barrel-proximal POTRA domain (P5) for stable interactions with BamA. We have previously reported that the BamA β-barrel assumes two different conformations. A method for conformation-specific labeling of BamA described here reveals that these conformers reflect the degree of surface exposure of the conserved sixth extracellular loop (L6). L6 is surface accessible in one conformation but not in the other, likely because it occupies the lumen of the BamA β-barrel in the latter case. A gain-of-function mutation that promotes Bam activity ( bamDR197L ) and a loss-of-function mutation that decreases the activity of Bam (Δ bamE ) both favor surface exposure of BamA L6, suggesting that BamD and BamE normally act to control L6 exposure through opposing functions. These results, along with the synthetic lethality of the bamDR197L Δ bamE double mutant, imply a cyclic mechanism in which the Bam lipoproteins regulate the conformation of BamA during the OMP assembly reaction. Our results further suggest that BamDE controls L6 exposure via conformational signals transmitted through P5 to L6." @default.
• W1994121837 created "2016-06-24" @default.
• W1994121837 creator A5007700514 @default.
• W1994121837 creator A5022582729 @default.
• W1994121837 creator A5029900874 @default.
• W1994121837 date "2013-03-11" @default.
• W1994121837 modified "2023-10-12" @default.
• W1994121837 title "Conformation-specific labeling of BamA and suppressor analysis suggest a cyclic mechanism for β-barrel assembly in <i>Escherichia coli</i>" @default.
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• W1994121837 doi "https://doi.org/10.1073/pnas.1302662110" @default.
• W1994121837 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3612609" @default.
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