ArticleProceedings of the National Academy of Sciences of the United States of America2013
Protease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 78 citations in OpenAlex.
- Stress-induced membrane insertion at the β-barrel assembly machinery complex regulates BepA metalloprotease activity.Nature communications · 2026Article
- Cryo-EM structures of the SurA-BAM complex reveal conformational changes in outer membrane protein assembly.Nature communications · 2026Article
- BAM-BepA complexes in outer membrane protein quality control.Nature communications · 2026Article
- Mutations affecting the β-sheet at the extracellular opening of the intimin β-barrel domain lead to reduced protein levels and inefficient passenger secretion.Bioscience reports · 2026Article
- Proteomics of long-term acclimation of the desert cyanobacteriumCurrent research in microbial sciences · 2026Article
- Pseudomonads coordinate innate defense against viruses and bacteria with a single regulatory system.Cell host & microbe · 2025Article
- Pseudomonads coordinate innate defense against viruses and bacteria with a single regulatory system.bioRxiv : the preprint server for biology · 2025Article
- AFM observation of protein translocation mediated by one unit of SecYEG-SecA complex.Nature communications · 2025Article
- Terrabacteria: redefining bacterial envelope diversity, biogenesis and evolution.Nature reviews. Microbiology · 2025Review
- The Transcriptomic Response of Cells of the Thermophilic BacteriumInternational journal of molecular sciences · 2024Article
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- Protein interactions in human pathogens revealed through deep learning.Nature microbiology · 2024Article
- The intrinsic macrolide resistome ofAntimicrobial agents and chemotherapy · 2024Article
- Co-evolution of gene transfer agents and their alphaproteobacterial hosts.Journal of bacteriology · 2024Article
- ATP-independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next-generation therapeutics.Protein science : a publication of the Protein Society · 2024Review
- Analysis of Transmembrane β-Barrel Proteins by Native and Semi-native Polyacrylamide Gel Electrophoresis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- LptM promotes oxidative maturation of the lipopolysaccharide translocon by substrate binding mimicry.Nature communications · 2023Article
- Article
- The sacrificial adaptor protein Skp functions to remove stalled substrates from the β-barrel assembly machine.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation.mBio · 2021Article
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gram-negative bacteria are equipped with quality-control systems for the outer membrane (OM) that sense and cope with defective biogenesis of its components. Accumulation of misfolded outer membrane proteins (OMPs) in Escherichia coli leads to activation of σ(E), an essential alternative σ factor that up-regulates transcription of multiple genes required to preserve OM structure and function. Disruption of bepA (formerly yfgC), a σ(E)-regulated gene encoding a putative periplasmic metalloprotease, sensitizes cells to multiple drugs, suggesting that it may be involved in maintaining OM integrity. However, the specific function of BepA remains unclear. Here, we show that BepA enhances biogenesis of LptD, an essential OMP involved in OM transport and assembly of lipopolysaccharide, by promoting rearrangement of intramolecular disulfide bonds of LptD. In addition, BepA possesses protease activity and is responsible for the degradation of incorrectly folded LptD. In the absence of periplasmic chaperone SurA, BepA also promotes degradation of BamA, the central OMP subunit of the β-barrel assembly machinery (BAM) complex. Interestingly, defective oxidative folding of LptD caused by bepA disruption was partially suppressed by expression of protease-active site mutants of BepA, suggesting that BepA functions independently of its protease activity. We also show that BepA has genetic and physical interaction with components of the BAM complex. These findings raised the possibility that BepA maintains the integrity of OM both by promoting assembly of OMPs and by proteolytically eliminating OMPs when their correct assembly was compromised.
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